Protein target profile

KP13_00983

NADH-quinone oxidoreductase subunit L

Genome: KpKP13 Gene: AHE43487.1 nuoL 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GT15

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Length 613

Pocket druggability 0.981

Direct ligand evidence 0 78 total records

Functional annotation 0 EC 6 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 0.98, P2Rank 0.54). 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 0.98. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.54. 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 (%): 39.332 Lower values reduce human off-target concern.
Human E-value: 2.43e-76
Gut microbiome similarity: 2.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 93.844 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: 96.75 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 0.981

Structure A0A0H3GT15

Pocket Pocket 39

P2Rank 0.537

Structure A0A0H3GT15

Pocket Pocket 1

ColabFold model

FPocket 0.966 · Pocket 39

P2Rank 0.554 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 133 / 4744 genomes with a hit

Prevalence 2.8%

Cross-references

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

Sequence

UniProt A0A0H3GT15

Sequence

Primary amino-acid sequence viewer.

MNMLALTILLPLIGFVLLAFSRGRWSENLSATVGMGSVGLAALVTAYVGVDFFANGKQAVSVPLWTWMSVGDFNIGFNLVLDGLSLTMLSVVTGVGFLIHMFASWYMRGEEGYSRFFAYTNLFIASMVVLVLADNLLLMYLGWEGVGLCSYLLIGFYYTDPKNGAAAMKAFVVTRVGDVFLAFALFILYNELGTLNFREMVELAPQHFANGSTTLQWATLMLLGGAVGKSAQLPLQTWLADAMAGPTPVSALIHAATMVTAGVYLIARTHGLFLMTPEVLHLVGIVGAVTLVLAGFAALVQTDIKRVLAYSTMSQIGYMFLALGVQAWDAAIFHLMTHAFFKALLFLSSGSVILACHHEQNIFKMGGLRKSIPLVYVCFLVGGAALSALPLITAGFFSKDEILAGAMANGHINLMVAGLVGAFMTSLYTFRMIFIVFHGKEQIHAHAGKGITHHLPLIVLLVLSTFVGALIVPPLEGVLPQTTELAHGSVMTLEIASGIIAIAGILIAAWLWLGKRTLVTSIANSAPGRFFGTWWFHAWGFDWLYDKVFVKPFLGIAWLLKRDPLNSLMNIPAILSRFAGKGLLVSENGYLRWYVASMSIGAVVVLALLMVLR

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

GO:0042773 The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP.
GO:0008137 Catalysis of the reaction: NADH + ubiquinone + 5 H+(in) = NAD+ + ubiquinol + 4 H+(out).
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:0003954 Catalysis of the reaction: NADH + H+ + acceptor = NAD+ + reduced acceptor.
GO:0048038 Binding to a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds.
GO:0015990 The transport of protons against an electrochemical gradient, using energy from electron transport.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

75 records

Show feature table

Start	End	DB	Term	Name
492	514	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
2	607	PANTHER	PTHR42829	NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5
2	607	InterPro	IPR003945	NADH-quinone oxidoreductase, chain 5-like
355	373	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
514	533	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
1	3	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
332	354	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
412	434	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
29	50	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	19	Phobius	SIGNAL_PEPTIDE	Signal peptide region
82	86	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
534	560	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
229	248	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
301	306	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
28	50	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
2	610	NCBIfam	TIGR01974	NADH-quinone oxidoreductase subunit L
2	610	InterPro	IPR018393	NADH-plastoquinone oxidoreductase, chain 5 subgroup
455	475	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
307	325	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
116	133	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
393	411	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
139	158	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
62	81	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
249	267	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
374	392	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
87	107	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
537	613	FunFam	G3DSA:1.20.5.2700:FF:000001	NADH-quinone oxidoreductase, L subunit
4	15	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
593	612	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
476	494	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
51	61	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
113	132	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
108	115	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
375	397	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
67	117	Pfam	PF00662	NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus
67	117	InterPro	IPR001516	NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal
455	477	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
209	228	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
495	513	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
16	19	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
170	189	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
538	613	Gene3D	G3DSA:1.20.5.2700	-
20	28	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	18	SignalP_EUK	SignalP-TM	SignalP-TM
159	169	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
435	454	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
613	613	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
244	266	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
58	82	PRINTS	PR01435	NADH-plastoquinone oxidoreductase chain 5 signature
84	104	PRINTS	PR01435	NADH-plastoquinone oxidoreductase chain 5 signature
358	380	PRINTS	PR01435	NADH-plastoquinone oxidoreductase chain 5 signature
417	439	PRINTS	PR01435	NADH-plastoquinone oxidoreductase chain 5 signature
561	592	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
4	21	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
268	278	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
84	106	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
279	301	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
247	273	PRINTS	PR01434	NADH-ubiquinone oxidoreductase chain 5 signature
110	130	PRINTS	PR01434	NADH-ubiquinone oxidoreductase chain 5 signature
157	178	PRINTS	PR01434	NADH-ubiquinone oxidoreductase chain 5 signature
225	246	PRINTS	PR01434	NADH-ubiquinone oxidoreductase chain 5 signature
418	437	PRINTS	PR01434	NADH-ubiquinone oxidoreductase chain 5 signature
82	107	PRINTS	PR01434	NADH-ubiquinone oxidoreductase chain 5 signature
315	327	PRINTS	PR01434	NADH-ubiquinone oxidoreductase chain 5 signature
331	354	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
133	425	Pfam	PF00361	Proton-conducting membrane transporter
133	425	InterPro	IPR001750	NADH:quinone oxidoreductase/Mrp antiporter, membrane subunit
412	434	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
134	138	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
136	158	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
590	612	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
326	330	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
190	208	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
171	193	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
279	300	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.

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 #39

0.981

Unusual size

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Surrounding area

Site 2 FPocket #11

0.591

Likely same site as P2Rank 1 1.4 Å 15 shared residues 75% of smaller site

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

0.537

Likely same site as FPocket 11 1.4 Å 15 shared residues 75% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.43

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Surrounding area

Site 3 P2Rank #3

0.269

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Surrounding area

Site 4 P2Rank #4

0.215

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Surrounding area

Site 5 P2Rank #5

0.191

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #39

0.966

Likely same site as P2Rank 4 2.3 Å 12 shared residues 92% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #28

0.86

Likely same site as P2Rank 2 1.3 Å 19 shared residues 90% of smaller site

Unusual size

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Surrounding area

Site 3 FPocket #6

0.554

Likely same site as P2Rank 1 2.9 Å 19 shared residues 95% of smaller site

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

0.554

Likely same site as FPocket 6 2.9 Å 19 shared residues 95% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.481

Likely same site as FPocket 28 1.3 Å 19 shared residues 90% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.24

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Surrounding area

Site 4 P2Rank #4

0.239

Likely same site as FPocket 39 2.3 Å 12 shared residues 92% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.171

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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_A0A0H3GT15	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00983	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.

78 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 28 records from similar proteins

Structural ligands 28 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

970 PDB via homolog Detail RCSB PDB

AYA PDB via homolog Detail RCSB PDB

BCR PDB via homolog Detail RCSB PDB

CDL 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	6QC2	O78756	748.1 Da LogP 12.06 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN)OC…`
970 RCSB PDB	6ZKL	O78756	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`CC(=C)[C@H]1Cc2c(ccc3c2O[C@@H]4COc5cc(c(cc5[C@@…`
AYA RCSB PDB	6ZKL	O78756	131.1 Da LogP -0.40 TPSA 66.4	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)NC(=O)C`
BCR RCSB PDB	6L7O	Q8DKX9	536.9 Da LogP 12.61 TPSA 0.0	2 viol.	✓ Clean	`CC1=C(C(CCC1)(C)C)\C=C\C(=C\C=C\C(=C\C=C\C=C(/C…`
CDL RCSB PDB	6RFR	Q9B6D3	1464.1 Da LogP 23.31 TPSA 242.6	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)([O-])OCC(…`
CPL RCSB PDB	6RFQ	Q9B6D3	758.1 Da LogP 10.94 TPSA 111.2	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)([O-])OC…`
DCQ RCSB PDB	6ZKA	O78756	322.4 Da LogP 4.49 TPSA 52.6	✓ Ro5	Alert	`CCCCCCCCCCC1=C(C(=O)C(=C(C1=O)OC)OC)C`
DGD RCSB PDB	6KHI	Q8DKX9	949.3 Da LogP 7.61 TPSA 231.1	4 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[C@H]1[C@@H]([C…`
EHZ RCSB PDB	6YJ4	Q9B6D3	584.7 Da LogP 3.04 TPSA 182.5	2 viol.	✓ Clean	`CCCCCCCCCCC[C@@H](CC(=O)SCCNC(=O)CCNC(=O)[C@@H]…`
FES RCSB PDB	6RFQ	Q9B6D3	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
FME RCSB PDB	6ZKL	O78756	177.2 Da LogP -0.06 TPSA 66.4	✓ Ro5	✓ Clean	`CSCC[C@@H](C(=O)O)NC=O`
LHG RCSB PDB	6KHI	Q8DKX9	723.0 Da LogP 9.89 TPSA 148.8	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@…`
LMG RCSB PDB	6HUM	Q8DKX9	787.2 Da LogP 9.78 TPSA 152.0	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[C@H]1[C@@H]([C…`
LMN RCSB PDB	6RFQ	Q9B6D3	1005.2 Da LogP -1.68 TPSA 357.1	3 viol.	✓ Clean	`CCCCCCCCCCC(CCCCCCCCCC)(CO[C@@H]1[C@@H]([C@@H](…`
LMT RCSB PDB	6YJ4	Q9B6D3	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1…`
MYR RCSB PDB	6ZKB	O78756	228.4 Da LogP 4.77 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)O`
PC1 RCSB PDB	7DGQ	P03920	790.2 Da LogP 12.17 TPSA 111.2	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)([O-])…`
PL9 RCSB PDB	6KHJ	Q8DKX9	749.2 Da LogP 16.57 TPSA 34.1	2 viol.	Alert	`CC1=C(C(=O)C(=CC1=O)CC=C(C)CCC=C(C)CCC=C(C)CCC=…`
PLC RCSB PDB	6RFQ	Q9B6D3	622.8 Da LogP 8.12 TPSA 108.4	2 viol.	✓ Clean	`CCCCCCCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)…`
PNS RCSB PDB	5LNK	O78756	358.4 Da LogP -0.96 TPSA 145.2	1 viol.	✓ Clean	`CC(C)(COP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCS)O`
PQN RCSB PDB	6L7P	Q8DKX9	450.7 Da LogP 9.16 TPSA 34.1	1 viol.	Alert	`CC1=C(C(=O)c2ccccc2C1=O)C\C=C(/C)\CCC[C@H](C)CC…`
PSC RCSB PDB	6Y79	Q9B6D3	759.1 Da LogP 11.58 TPSA 108.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCC[N…`
SQD RCSB PDB	6KHI	Q8DKX9	795.1 Da LogP 8.12 TPSA 186.1	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](COC1[C@@H]([C@H]([C…`
T7X RCSB PDB	6RFR	Q9B6D3	887.1 Da LogP 9.17 TPSA 209.5	4 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OC1[C@@…`
UMQ RCSB PDB	4HE8	Q56227	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1)…`
UQ2 RCSB PDB	7DGQ	P03920	318.4 Da LogP 4.04 TPSA 52.6	✓ Ro5	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)C\C=C(/C)\CCC=C(C)C`
UQ9 RCSB PDB	6RFR	Q9B6D3	795.2 Da LogP 16.13 TPSA 52.6	2 viol.	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)C\C=C(/C)\CC\C=C(/C)…`
ZMP RCSB PDB	5LNK	O78756	568.7 Da LogP 4.07 TPSA 162.3	1 viol.	✓ Clean	`CCCCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@H](C(C)(C…`

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
ZINC102191119 ZINC	1.000	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](O)CO…`
ZINC13522091 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)…`
ZINC1529498 ZINC	1.000	200.3 Da LogP 3.99 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)O`
ZINC1530417 ZINC	1.000	228.4 Da LogP 4.77 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)O`
ZINC1530836 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)c…`
ZINC1628119 ZINC	1.000	214.3 Da LogP 4.38 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)O`
ZINC2548962 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)c…`
ZINC3860715 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)c…`
ZINC3874884 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)…`
ZINC3874885 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)cc…`
ZINC58649551 ZINC	1.000	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](O)CO)…`
ZINC8660420 ZINC	1.000	394.4 Da LogP 3.70 TPSA 63.2	✓ Ro5	✓ Clean	`C=C(C)[C@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)c…`
ZINC226792912 ZINC	0.860	396.4 Da LogP 2.72 TPSA 80.3	✓ Ro5	✓ Clean	`COc1cc2c(cc1OC)[C@@H]1C(=O)c3ccc4c(c3O[C@@H]1CO…`
ZINC226792928 ZINC	0.860	396.4 Da LogP 2.72 TPSA 80.3	✓ Ro5	✓ Clean	`COc1cc2c(cc1OC)[C@@H]1C(=O)c3ccc4c(c3O[C@H]1CO2…`
ZINC230121190 ZINC	0.860	396.4 Da LogP 2.72 TPSA 80.3	✓ Ro5	✓ Clean	`COc1cc2c(cc1OC)[C@@H]1C(=O)c3ccc4c(c3O[C@@H]1CO…`
ZINC230121201 ZINC	0.860	396.4 Da LogP 2.72 TPSA 80.3	✓ Ro5	✓ Clean	`COc1cc2c(cc1OC)[C@@H]1C(=O)c3ccc4c(c3O[C@H]1CO2…`
ZINC138457918 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCC(=O)O`
ZINC138458029 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCC(=O)O`
ZINC144395054 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCCC(=O)O`
ZINC14619628 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCCCCC(=O)O`
ZINC196749828 ZINC	0.850	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCC(=O)O`
ZINC2113934076 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCCC(=O)O`
ZINC2113934082 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCCCC(=O)O`
ZINC2113934083 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)CCCCC(=O)O`
ZINC2243670 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCC(=O)O`
ZINC2569203 ZINC	0.850	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCC(=O)O`
ZINC4798470 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC5973005 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCC(=O)O`
ZINC71418182 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCC(=O)CCCCC(=O)O`
ZINC79244776 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCCCCC(=O)O`
ZINC86037082 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)CCCCCC(=O)O`
ZINC86037089 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCCCCCC(=O)O`
ZINC86039283 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCCCC(=O)O`
ZINC13813085 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)…`
ZINC13813088 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC…`
ZINC2115043 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC…`
ZINC36387001 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@@H]1Cc2c(ccc3c2O[C@H]2COc4cc(OC)c(OC)…`
ZINC3947515 ZINC	0.820	410.4 Da LogP 2.68 TPSA 83.5	✓ Ro5	✓ Clean	`C=C(CO)[C@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC)c(OC)…`
ZINC2242696 ZINC	0.810	273.3 Da LogP -1.39 TPSA 124.6	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C…`
ZINC2566274 ZINC	0.810	344.4 Da LogP -1.89 TPSA 153.7	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C…`
ZINC2572098 ZINC	0.810	202.2 Da LogP -0.90 TPSA 95.5	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)O`
ZINC3160730 ZINC	0.810	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCC(=O)O`
ZINC4582907 ZINC	0.810	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCC(=O)O`
ZINC4727003 ZINC	0.810	312.4 Da LogP 4.69 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCC(=O)CCCCCCCC(=O)O`
ZINC5706638 ZINC	0.810	344.4 Da LogP -1.89 TPSA 153.7	✓ Ro5	✓ Clean	`CC(=O)N[C@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(…`
ZINC5706639 ZINC	0.810	344.4 Da LogP -1.89 TPSA 153.7	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C)C(=O)N[C@H](C)C(=O)N[C@@H](C)C(…`
ZINC5706640 ZINC	0.810	344.4 Da LogP -1.89 TPSA 153.7	✓ Ro5	✓ Clean	`CC(=O)N[C@H](C)C(=O)N[C@H](C)C(=O)N[C@@H](C)C(=…`
ZINC86037074 ZINC	0.810	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)CCCC(=O)O`
ZINC2378801 ZINC	0.800	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCC(=O)O`
ZINC12364517 ZINC	0.797	452.5 Da LogP 3.25 TPSA 89.5	✓ Ro5	✓ Clean	`C=C(COC(C)=O)[C@H]1Cc2c(ccc3c2O[C@@H]2COc4cc(OC…`

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.