Protein target profile

KP13_03684

Ubiquinol oxidase subunit 1

Genome: KpKP13 Gene: cyoB AHE46024.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GNJ6

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Length 663

Pocket druggability 0.998

Direct ligand evidence 0 89 total records

Functional annotation 1 EC 10 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 1.00, P2Rank 1.00). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 1.00. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 1.00. Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: Hit
Human identity (%): 39.139 Lower values reduce human off-target concern.
Human E-value: 9.23e-109
Gut microbiome similarity: 4.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 50.24 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 96.93 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.998

Structure A0A0H3GNJ6

Pocket Pocket 26

P2Rank 0.999

Structure A0A0H3GNJ6

Pocket Pocket 1

ColabFold model

FPocket 0.997 · Pocket 1

P2Rank 0.999 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 214 / 4744 genomes with a hit

Prevalence 4.5%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GNJ6

Chemistry

ChEMBL CHEMBL1774043 ChEMBL CHEMBL1773877 ChEMBL CHEMBL441414 ChEMBL CHEMBL5568511 ChEMBL CHEMBL1200699 ChEMBL CHEMBL4744682 ChEMBL CHEMBL4760290 ChEMBL CHEMBL4795726 ChEMBL CHEMBL4798758

Sequence

Primary amino-acid sequence viewer.

MFGKLTLDAVPYHEPIIVVTVAAIIIGGLALLAAITYFGKWSYLWNEWLTSVDHKRLGIMYVIVAIVMLLRGFADAIMMRSQQVLASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQLGARDVAFPFLNNLSFWFTVVGVILVNLSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWALQLSGIGTTLTGINFFVTIIKMRAPGMTMFKMPVFSWASLCANILIIASFPILTVTIALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILVLPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFNSAMMWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWWPKAFGFTLNETWGKRAFWFWIIGFFVAFMPLYVLGFMGMTRRLSQQIDPQFHPMLVIAACGAALIACGILCQLIQFYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAIVPQVHERDAFWEMKEKGEAYKQPAHYEEIHMPKNSGAGIVIAAFATVFGFAMIWHIWWMAIASFIGIVATWIIKSFDEDVDYYVPVAEVEKLEKQHFDEINKAGLKNGN

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

7.1.1.3

Gene Ontology (GO)

GO:0009060 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which requires oxygen as the terminal electron acceptor.
GO:0016682 Catalysis of an oxidation-reduction (redox) reaction in which a diphenol, or related compound, acts as a hydrogen or electron donor and reduces oxygen.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0004129 Catalysis of the reaction: 4 Fe(II)-[cytochrome c] + O2 + 8 H+(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H+(out).
GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0009486 Catalysis of the reaction: 2 ubiquinol + O2 + 4 H+ = 2 ubiquinone + 2 H2O + 4 H+ [periplasmic space].
GO:0046872 Binding to a metal ion.
GO:0015990 The transport of protons against an electrochemical gradient, using energy from electron transport.
GO:0022904 A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

83 records

Show feature table

Start	End	DB	Term	Name
437	456	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
256	274	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
404	414	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
214	232	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
628	663	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
146	170	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
140	162	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
56	503	Pfam	PF00115	Cytochrome C and Quinol oxidase polypeptide I
56	503	InterPro	IPR000883	Cytochrome c oxidase subunit I
15	37	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	15	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
59	79	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
103	126	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
191	213	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
491	518	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
275	298	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
39	58	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
480	490	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
57	79	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
45	567	PANTHER	PTHR10422	CYTOCHROME C OXIDASE SUBUNIT 1
45	567	InterPro	IPR000883	Cytochrome c oxidase subunit I
105	127	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
594	627	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
233	255	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
415	436	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
457	479	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
39	559	ProSiteProfiles	PS50855	Cytochrome oxidase subunit I profile.
39	559	InterPro	IPR023616	Cytochrome c oxidase-like, subunit I domain
310	332	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
127	145	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
275	297	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
171	189	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
16	38	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
519	593	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
335	345	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
380	403	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
346	368	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
80	102	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
52	552	FunFam	G3DSA:1.20.210.10:FF:000002	Cytochrome o ubiquinol oxidase, subunit I
233	255	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
347	369	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
48	552	CDD	cd01662	Ubiquinol_Oxidase_I
280	334	ProSitePatterns	PS00077	Heme-copper oxidase catalytic subunit, copper B binding region signature.
280	334	InterPro	IPR023615	Cytochrome c oxidase, subunit I, copper-binding site
299	309	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
457	479	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
494	516	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
227	246	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
227	246	InterPro	IPR000883	Cytochrome c oxidase subunit I
124	148	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
124	148	InterPro	IPR000883	Cytochrome c oxidase subunit I
383	401	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
383	401	InterPro	IPR000883	Cytochrome c oxidase subunit I
198	216	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
198	216	InterPro	IPR000883	Cytochrome c oxidase subunit I
47	72	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
47	72	InterPro	IPR000883	Cytochrome c oxidase subunit I
97	120	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
97	120	InterPro	IPR000883	Cytochrome c oxidase subunit I
278	299	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
278	299	InterPro	IPR000883	Cytochrome c oxidase subunit I
411	430	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
411	430	InterPro	IPR000883	Cytochrome c oxidase subunit I
166	178	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
166	178	InterPro	IPR000883	Cytochrome c oxidase subunit I
324	339	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
324	339	InterPro	IPR000883	Cytochrome c oxidase subunit I
461	482	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
461	482	InterPro	IPR000883	Cytochrome c oxidase subunit I
348	369	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
348	369	InterPro	IPR000883	Cytochrome c oxidase subunit I
2	647	NCBIfam	TIGR02843	cytochrome o ubiquinol oxidase subunit I
2	647	InterPro	IPR014207	Cytochrome o ubiquinol oxidase, subunit I
590	612	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
310	334	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
382	404	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
43	559	SUPERFAMILY	SSF81442	Cytochrome c oxidase subunit I-like
43	559	InterPro	IPR036927	Cytochrome c oxidase-like, subunit I superfamily
190	213	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
369	379	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
414	436	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
52	552	Gene3D	G3DSA:1.20.210.10	-
52	552	InterPro	IPR036927	Cytochrome c oxidase-like, subunit I superfamily

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #26

0.998

Likely same site as P2Rank 1 0.8 Å 64 shared residues 96% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #42

0.822

Likely same site as P2Rank 4 2.1 Å 12 shared residues 100% of smaller site

Unusual size

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Surrounding area

Site 3 FPocket #33

0.502

Likely same site as P2Rank 5 1.8 Å 14 shared residues 93% of smaller site

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Surrounding area

Site 4 FPocket #4

0.233

Unusual size

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.999

Likely same site as FPocket 26 0.8 Å 64 shared residues 96% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.56

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Surrounding area

Site 3 P2Rank #3

0.546

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Surrounding area

Site 4 P2Rank #4

0.416

Likely same site as FPocket 42 2.1 Å 12 shared residues 100% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.413

Likely same site as FPocket 33 1.8 Å 14 shared residues 93% of smaller site

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Surrounding area

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #1

0.997

Likely same site as P2Rank 1 0.4 Å 54 shared residues 93% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #39

0.987

Likely same site as P2Rank 5 4.4 Å 17 shared residues 94% of smaller site

Unusual size

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Surrounding area

Site 3 FPocket #22

0.336

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Surrounding area

Site 4 FPocket #21

0.243

Likely same site as P2Rank 4 1.3 Å 12 shared residues 86% of smaller site

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.999

Likely same site as FPocket 1 0.4 Å 54 shared residues 93% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.705

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Surrounding area

Site 3 P2Rank #3

0.436

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Surrounding area

Site 4 P2Rank #4

0.417

Likely same site as FPocket 21 1.3 Å 12 shared residues 86% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.393

Likely same site as FPocket 39 4.4 Å 17 shared residues 94% of smaller site

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3GNJ6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03684	ColabFold	—	—	full sequence	—	Loaded

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

89 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 39 records from similar proteins

Structural ligands 30 0 loaded crystals

Measured bioactivity 9 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3PE PDB via homolog 748.1 Da · LogP 12.06 · TPSA 134.4 Open detail RCSB PDB

4AG PDB via homolog Detail RCSB PDB

5PL PDB via homolog Detail RCSB PDB

7E8 PDB via homolog Detail RCSB PDB

7E9 PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
3PE RCSB PDB	6WTI	P0ABI8	748.1 Da LogP 12.06 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN)OC…`
4AG RCSB PDB	2YEV	P98005	568.9 Da LogP 10.40 TPSA 72.8	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](CO)OC(=O)CCCCCCCCC…`
5PL RCSB PDB	2YEV	P98005	1233.7 Da LogP 15.13 TPSA 245.7	4 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCCCNC(=O)[C@@H](CO[C@@H]1[C@@H]…`
7E8 RCSB PDB	2YEV	P98005	300.4 Da LogP 3.36 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCC(=O)OC[C@@H](CO)O`
7E9 RCSB PDB	2YEV	P98005	300.4 Da LogP 3.36 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCC(=O)OC(CO)CO`
AZI RCSB PDB	1OCZ	P00396	42.0 Da LogP 0.87 TPSA 58.7	✓ Ro5	Alert	`[N-]=[N+]=[N-]`
CDL RCSB PDB	6HWH	A0R0M4	1464.1 Da LogP 23.31 TPSA 242.6	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)([O-])OCC(…`
CHD RCSB PDB	1V54	P00396	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@@H]2[C@@]1([C@H](C[C…`
CMO RCSB PDB	1OCO	P00396	28.0 Da LogP -0.04 TPSA 19.9	✓ Ro5	✓ Clean	`[C-]#[O+]`
CQX RCSB PDB	6JY3	P00396	364.5 Da LogP 0.96 TPSA 108.6	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCO[C@@H]1[C@H]([C@H]([C@@H]([C@H](O…`
CUA RCSB PDB	1V54	P00396	127.1 Da LogP -0.01 TPSA 0.0	✓ Ro5	✓ Clean	`[Cu][Cu]`
DCW RCSB PDB	2DYS	P00396	224.3 Da LogP 2.95 TPSA 41.1	✓ Ro5	✓ Clean	`C1CCC(CC1)NC(=O)NC2CCCCC2`
DMU RCSB PDB	1V54	P00396	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1)C…`
FES RCSB PDB	6HWH	A0R0M4	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
FME RCSB PDB	5WAU	P00396	177.2 Da LogP -0.06 TPSA 66.4	✓ Ro5	✓ Clean	`CSCC[C@@H](C(=O)O)NC=O`
HEO RCSB PDB	1FFT	P0ABI8	838.9 Da LogP 8.07 TPSA 110.7	2 viol.	✓ Clean	`Cc1c2cc3[n+]4c(cc5c(c(c6n5[Fe]47n2c(c1CCC(=O)O)…`
HQO RCSB PDB	6KOE	P34956	259.3 Da LogP 3.69 TPSA 47.2	✓ Ro5	Alert	`CCCCCCCc1cc(c2ccccc2[n+]1[O-])O`
IHQ RCSB PDB	6KOC	P34956	385.2 Da LogP 4.36 TPSA 42.2	✓ Ro5	✓ Clean	`CCCCCCCC1=C(C(=O)c2ccccc2N1O)I`
MQ7 RCSB PDB	6KOB	P34956	649.0 Da LogP 14.10 TPSA 34.1	2 viol.	Alert	`CC1=C(C(=O)c2ccccc2C1=O)C\C=C(/C)\CC\C=C(/C)\CC…`
MQ9 RCSB PDB	6HWH	A0R0M4	785.3 Da LogP 17.55 TPSA 34.1	2 viol.	Alert	`CC1=C(C(=O)c2ccccc2C1=O)C\C=C(/C)\CC\C=C(/C)\CC…`
O RCSB PDB	6NKN	P00396	18.0 Da LogP -0.82 TPSA 31.5	✓ Ro5	✓ Clean	`O`
OXY RCSB PDB	2Y69	P00396	32.0 Da LogP 0.07 TPSA 34.1	✓ Ro5	✓ Clean	`O=O`
PEE RCSB PDB	5Z62	P00395	744.0 Da LogP 11.61 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCC/C=C\CCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN…`
PEK RCSB PDB	1V54	P00396	768.1 Da LogP 11.94 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN…`
PER RCSB PDB	2OCC	P00396	32.0 Da LogP -2.38 TPSA 46.1	✓ Ro5	✓ Clean	`[O-][O-]`
PGV RCSB PDB	1V54	P00396	749.0 Da LogP 10.45 TPSA 148.8	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OC[C@H…`
PSC RCSB PDB	1V54	P00396	759.1 Da LogP 11.58 TPSA 108.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCC[N…`
TGL RCSB PDB	1V54	P00396	891.5 Da LogP 18.77 TPSA 78.9	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OCC(COC(=O)CCCCCCCCCCCCCC…`
U9V RCSB PDB	6WTI	P0ABI8	524.9 Da LogP 10.65 TPSA 52.6	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OCCOC(=O)CCCCCCCCCCCCCC`
UQ8 RCSB PDB	6WTI	P0ABI8	727.1 Da LogP 14.40 TPSA 52.6	2 viol.	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)CC=C(C)CC\C=C(/C)\CC…`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL1774043 ChEMBL	P00395	6.89 ~128.8 nM	576.6 Da LogP 6.08 TPSA 95.9	2 viol.	✓ Clean	`COc1ccc(-c2cnc(C(=O)N3CCN(c4cc(C(=O)O)c5ccccc5c…`
CHEMBL1773877 ChEMBL	P00395	6.62 ~239.9 nM	604.6 Da LogP 5.84 TPSA 105.1	2 viol.	✓ Clean	`Cc1ccc(-c2nc(C(=O)N3CCN(c4cc(C(=O)O)c5ccccc5c4)…`
CHEMBL441414 ChEMBL	P00395	6.55 ~281.8 nM	248.3 Da LogP 2.58 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)c1ccc(C[C@H]2CCC[C@@H]2O)cc1`
CHEMBL5568511 ChEMBL	P00395	6.49 ~323.6 nM	337.4 Da LogP 2.85 TPSA 87.4	✓ Ro5	Alert	`CCc1nn(-c2ccccc2)c(O)c1Cc1ccc(C(=O)NO)cc1`
CHEMBL1200699 ChEMBL	P00395	—	462.5 Da LogP -1.17 TPSA 213.1	1 viol.	✓ Clean	`C[C@H]1c2cccc(O)c2C(=O)C2=C(O)[C@]3(O)C(=O)C(C(…`
CHEMBL4744682 ChEMBL	P00395	—	896.4 Da LogP 2.32 TPSA 210.7	2 viol.	✓ Clean	`C[C@H]1c2ccc(NC(=O)CCCCCCCC[P+](c3ccccc3)(c3ccc…`
CHEMBL4760290 ChEMBL	P00395	—	924.5 Da LogP 3.10 TPSA 210.7	2 viol.	✓ Clean	`C[C@H]1c2ccc(NC(=O)CCCCCCCCCC[P+](c3ccccc3)(c3c…`
CHEMBL4795726 ChEMBL	P00395	—	1323.5 Da LogP 12.07 TPSA 197.2	3 viol.	✓ Clean	`CC[C@H]1OC(=O)[C@H](C)[C@@H](O[C@H]2C[C@@](C)(O…`
CHEMBL4798758 ChEMBL	P00395	—	938.5 Da LogP 3.49 TPSA 210.7	2 viol.	✓ Clean	`C[C@H]1c2ccc(NC(=O)CCCCCCCCCCC[P+](c3ccccc3)(c3…`

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC100028164 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)O)[C@H]1CC[C@H]2[C@H]3[C@H](C[C@…`
ZINC100053689 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H]…`
ZINC102190506 ZINC	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512 ZINC	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC118912549 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@H]2[C@H]3[C@H](C[C@@…`
ZINC118912550 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)O)[C@H]1CC[C@H]2[C@H]3[C@H](C[C@…`
ZINC118914076 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)O)[C@H]1CC[C@H]2[C@H]3[C@H](C[C@…`
ZINC1501015302 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC1636271 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@@H]3[C@H](O)…`
ZINC17654071 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@H]2[C@@H]3[C@H](O)C[…`
ZINC17654239 ZINC	1.000	314.5 Da LogP 4.79 TPSA 52.6	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCCOC(=O)CCCCCCC`
ZINC1857524335 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)O)[C@@H]1CC[C@H]2[C@H]3[C@H](C[C…`
ZINC1857524336 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@@H]1CC[C@H]2[C@H]3[C@H](C[C@…`
ZINC2053493147 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493148 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493149 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2060993462 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)O)[C@@H]1CC[C@H]2[C@@H]3[C@H](O)…`
ZINC2060993463 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)O)[C@@H]1CC[C@H]2[C@@H]3[C@H](O)…`
ZINC2060993464 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)O)[C@@H]1CC[C@H]2[C@@H]3[C@H](O)…`
ZINC245204447 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@H]3[C@H](O)C…`
ZINC245239737 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@H]3[C@H](O)C…`
ZINC252695223 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695225 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC253497472 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@H]3[C@H](O)…`
ZINC253497473 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@H]3[C@H](O)C…`
ZINC253497474 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@H]3[C@H](O)…`
ZINC253497475 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@H]3[C@H](O)C…`
ZINC253536099 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@@H]3[C@H](C…`
ZINC257345209 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@@H]2[C@H]3[C@H](O)C[…`
ZINC257354841 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@H]3[C@H](C[C…`
ZINC257360748 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@@H]3[C@H](C[…`
ZINC28218857 ZINC	1.000	248.3 Da LogP 2.58 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)c1ccc(C[C@H]2CCC[C@@H]2O)cc1`
ZINC28220807 ZINC	1.000	248.3 Da LogP 2.58 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)c1ccc(C[C@H]2CCC[C@@H]2O)cc1`
ZINC29747682 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@H]2[C@H]3[C@H](C[C@H…`
ZINC370205 ZINC	1.000	252.4 Da LogP 3.73 TPSA 41.1	✓ Ro5	✓ Clean	`O=C(NC1CCCCCCC1)NC1CCCCC1`
ZINC376044 ZINC	1.000	238.4 Da LogP 3.34 TPSA 41.1	✓ Ro5	✓ Clean	`O=C(NC1CCCCCC1)NC1CCCCC1`
ZINC40164313 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@H]2[C@@H]3[C@@H](O)C…`
ZINC43352176 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)O)[C@@H]1CC[C@H]2[C@H]3[C@H](C[C…`
ZINC44123745 ZINC	1.000	252.4 Da LogP 3.73 TPSA 41.1	✓ Ro5	✓ Clean	`O=C(NC1CCCCCC1)NC1CCCCCC1`
ZINC59978443 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](…`
ZINC6858022 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@H]2[C@H]3[C@H](C[C@H…`
ZINC70669940 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669941 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669943 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70691804 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@@H]2[C@@H]3[C@H](O)C…`
ZINC70691805 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@@H]2[C@H]3[C@H](C[C@…`
ZINC8214946 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@@H]2[C@H]3[C@H](O)C[…`
ZINC8214947 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@H]2[C@@H]3[C@H](C[C@…`
ZINC85603116 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@@H]2[C@@H]3[C@H](C[C…`
ZINC95099755 ZINC	1.000	408.6 Da LogP 3.45 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@H]3[C@H](O)…`

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.