Protein target profile

VK055_2161

cytochrome o ubiquinol oxidase, subunit I

Genome: KpATCC43816 Gene: AIK80766.1 cyoB 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GNJ6

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Length 604

Pocket druggability 0.998

Direct ligand evidence 0 83 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 1.00. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 33 structural and 0 bioactivity records.

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 (%): 40.126 Lower values reduce human off-target concern.
Human E-value: 2.77e-104
Gut microbiome similarity: 4.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 49.663 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: 97.28 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 0.996 · Pocket 2

P2Rank 0.999 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 215 / 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

Sequence

Primary amino-acid sequence viewer.

MYVIVAIVMLLRGFADAIMMRSQQVLASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQLGARDVAFPFLNNLSFWFTVVGVILVNLSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWALQLSGIGTTLTGINFFVTIIKMRAPGMTMFKMPVFSWASLCANILIIASFPILTVTIALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILVLPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFNSAMMWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWWPKAFGFTLNETWGKRAFWFWIIGFFVAFMPLYVLGFMGMTRRLSQQIDPQFHPMLVIAACGAALIACGILCQLIQFYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAIVPQVHERDAFWEMKEKGEAYKQPAHYEEIHMPKNSGAGIVIAAFATVFGFAMIWHIWWMAIASFIGIVATWIIKSFDEDVDYYVPVAEVEKLEKQHFDEINKAGLKNGN

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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
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: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: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: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.

80 records

Show feature table

Start	End	DB	Term	Name
3	11	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
288	310	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
321	344	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	493	FunFam	G3DSA:1.20.210.10:FF:000002	Cytochrome o ubiquinol oxidase, subunit I
112	130	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	17	SignalP_EUK	SignalP-TM	SignalP-TM
356	377	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
216	239	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
421	431	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
132	154	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
87	111	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
398	420	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
221	275	ProSitePatterns	PS00077	Heme-copper oxidase catalytic subunit, copper B binding region signature.
221	275	InterPro	IPR023615	Cytochrome c oxidase, subunit I, copper-binding site
155	173	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
81	103	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	531	SUPERFAMILY	SSF81442	Cytochrome c oxidase subunit I-like
1	531	InterPro	IPR036927	Cytochrome c oxidase-like, subunit I superfamily
174	196	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
432	459	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
46	68	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
251	273	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	493	CDD	cd01662	Ubiquinol_Oxidase_I
30	44	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
569	604	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
345	355	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
378	397	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
1	444	Pfam	PF00115	Cytochrome C and Quinol oxidase polypeptide I
1	444	InterPro	IPR000883	Cytochrome c oxidase subunit I
1	500	ProSiteProfiles	PS50855	Cytochrome oxidase subunit I profile.
1	500	InterPro	IPR023616	Cytochrome c oxidase-like, subunit I domain
251	275	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
310	320	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
197	215	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
216	238	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
174	196	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
45	67	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
131	154	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
240	250	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
1	588	NCBIfam	TIGR02843	cytochrome o ubiquinol oxidase subunit I
1	588	InterPro	IPR014207	Cytochrome o ubiquinol oxidase, subunit I
398	420	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	508	PANTHER	PTHR10422	CYTOCHROME C OXIDASE SUBUNIT 1
1	508	InterPro	IPR000883	Cytochrome c oxidase subunit I
68	86	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
1	2	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
1	493	Gene3D	G3DSA:1.20.210.10	-
1	493	InterPro	IPR036927	Cytochrome c oxidase-like, subunit I superfamily
531	553	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
12	29	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
435	457	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
276	286	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
460	534	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
323	345	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
355	377	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
287	309	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	29	Phobius	SIGNAL_PEPTIDE	Signal peptide region
535	568	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
65	89	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
65	89	InterPro	IPR000883	Cytochrome c oxidase subunit I
139	157	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
139	157	InterPro	IPR000883	Cytochrome c oxidase subunit I
168	187	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
168	187	InterPro	IPR000883	Cytochrome c oxidase subunit I
324	342	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
324	342	InterPro	IPR000883	Cytochrome c oxidase subunit I
107	119	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
107	119	InterPro	IPR000883	Cytochrome c oxidase subunit I
352	371	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
352	371	InterPro	IPR000883	Cytochrome c oxidase subunit I
402	423	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
402	423	InterPro	IPR000883	Cytochrome c oxidase subunit I
38	61	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
38	61	InterPro	IPR000883	Cytochrome c oxidase subunit I
265	280	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
265	280	InterPro	IPR000883	Cytochrome c oxidase subunit I
289	310	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
289	310	InterPro	IPR000883	Cytochrome c oxidase subunit I
219	240	PRINTS	PR01165	Cytochrome c oxidase subunit I signature
219	240	InterPro	IPR000883	Cytochrome c oxidase subunit I

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 · P2Rank

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

Site 1 P2Rank #1

0.999

Likely same site as FPocket 2 2.0 Å 57 shared residues 89% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.605

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Surrounding area

Site 3 P2Rank #3

0.494

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Surrounding area

Site 4 P2Rank #4

0.489

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Surrounding area

Site 5 P2Rank #5

0.089

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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 VK055_2161	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.

83 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 33 records from similar proteins

Structural ligands 33 0 loaded crystals

Measured bioactivity 0 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	2GSM	P33517	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…`
DXC RCSB PDB	3DTU	P33517	392.6 Da LogP 4.48 TPSA 77.8	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@@H]2[C@@]1([C@H](C[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`
HTO RCSB PDB	3DTU	P33517	148.2 Da LogP -0.11 TPSA 60.7	✓ Ro5	✓ Clean	`CCCC[C@H]([C@@H](CO)O)O`
IHQ RCSB PDB	6KOC	P34956	385.2 Da LogP 4.36 TPSA 42.2	✓ Ro5	✓ Clean	`CCCCCCCC1=C(C(=O)c2ccccc2N1O)I`
LMU RCSB PDB	5WEH	P33517	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1[C@@H]([C@H]([C@@H]([C@H](O…`
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`
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…`
TRD RCSB PDB	2GSM	P33517	184.4 Da LogP 5.32 TPSA 0.0	1 viol.	✓ Clean	`CCCCCCCCCCCCC`
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).

No ChEMBL hits found through similar proteins.

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
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]…`
ZINC100053691 ZINC	1.000	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[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…`
ZINC12493596 ZINC	1.000	392.6 Da LogP 4.48 TPSA 77.8	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@H]1CC[C@H]2[C@@H]3CC[C@H]4C[…`
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…`
ZINC1529909 ZINC	1.000	259.3 Da LogP 3.69 TPSA 47.2	✓ Ro5	Alert	`CCCCCCCc1cc(O)c2ccccc2[n+]1[O-]`
ZINC157375 ZINC	1.000	224.3 Da LogP 2.95 TPSA 41.1	✓ Ro5	✓ Clean	`O=C(NC1CCCCC1)NC1CCCCC1`
ZINC17654239 ZINC	1.000	314.5 Da LogP 4.79 TPSA 52.6	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCCOC(=O)CCCCCCC`
ZINC2039285652 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](C…`
ZINC2039285653 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](C…`
ZINC2039285654 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](C…`
ZINC2039285655 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](C…`
ZINC2053493146 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]…`
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]…`
ZINC238809244 ZINC	1.000	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C…`
ZINC238809245 ZINC	1.000	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[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…`
ZINC252695224 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…`
ZINC252695226 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…`
ZINC257356883 ZINC	1.000	392.6 Da LogP 4.48 TPSA 77.8	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@@H]3CC[C@H]4…`
ZINC257356885 ZINC	1.000	392.6 Da LogP 4.48 TPSA 77.8	✓ Ro5	✓ Clean	`C[C@H](CCC(=O)O)[C@@H]1CC[C@@H]2[C@@H]3CC[C@H]4…`
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`
ZINC44123745 ZINC	1.000	252.4 Da LogP 3.73 TPSA 41.1	✓ Ro5	✓ Clean	`O=C(NC1CCCCCC1)NC1CCCCCC1`
ZINC58649715 ZINC	1.000	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@…`
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](…`
ZINC66157001 ZINC	1.000	468.5 Da LogP -1.62 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[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@…`
ZINC70669942 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@…`
ZINC77311968 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]…`
ZINC83433913 ZINC	1.000	426.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](CO…`
ZINC85482724 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…`
ZINC86002923 ZINC	1.000	426.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@H](O[C@H]2O[C@H](CO)…`
ZINC27416437 ZINC	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364 ZINC	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC1532641 ZINC	0.972	318.4 Da LogP 4.04 TPSA 52.6	✓ Ro5	Alert	`COC1=C(OC)C(=O)C(C/C=C(\C)CCC=C(C)C)=C(C)C1=O`
ZINC4691823 ZINC	0.952	258.4 Da LogP 3.23 TPSA 52.6	✓ Ro5	✓ Clean	`CCCCCC(=O)OCCOC(=O)CCCCC`
ZINC48844720 ZINC	0.944	210.3 Da LogP 2.56 TPSA 41.1	✓ Ro5	✓ Clean	`O=C(NC1CCCCCCC1)NC1CC1`
ZINC100302690 ZINC	0.875	258.4 Da LogP 4.10 TPSA 35.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OCCOC`
ZINC101034896 ZINC	0.875	402.6 Da LogP 4.83 TPSA 71.1	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCCOCCOCCOC(=O)CCCCCCC`
ZINC206748657 ZINC	0.875	374.5 Da LogP 4.05 TPSA 71.1	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCCOCCOCCOC(=O)CCCCC`
ZINC218215426 ZINC	0.875	402.6 Da LogP 4.83 TPSA 71.1	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)OCCOCCOCCOC(=O)CCCCC`
ZINC1608718 ZINC	0.870	214.3 Da LogP 4.08 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCCCCC`
ZINC2516185 ZINC	0.870	214.3 Da LogP 4.08 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)OCCC`

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.