Protein target profile

KP13_31481

Fumarate reductase flavoprotein subunit

Genome: KpKP13 Gene: frdA AHE46751.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GI02

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Length 596

Pocket druggability 0.997

Direct ligand evidence 0 86 total records

Functional annotation 1 EC 9 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 0.97). 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 0.97. 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 (%): 43.99 Lower values reduce human off-target concern.
Human E-value: 2.57e-100
Gut microbiome similarity: 3.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 54.352 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: 96.29 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 0.997

Structure A0A0H3GI02

Pocket Pocket 1

P2Rank 0.975

Structure A0A0H3GI02

Pocket Pocket 1

ColabFold model

FPocket 0.737 · Pocket 1

P2Rank 0.983 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 157 / 4744 genomes with a hit

Prevalence 3.3%

Cross-references

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

Sequence

UniProt A0A0H3GI02

Sequence

Primary amino-acid sequence viewer.

MQTFQADLAVIGAGGAGLRAAIAAAQANPNAKIALISKVYPMRSHTVAAEGGSAAVAQDHDSFEYHFHDTVAGGDWLCEQDVVDYFVHHCPTEMTQLEQWGCPWSRRPDGSVNVRRFGGMKIERTWFAADKTGFHMLHTLFQTSLQFPQIQRFDEHFVLDLLVDDGLARGLVAMNMMEGTLVQIRANAVVLATGGAGRVYRYNTNGGIVTGDGMGMALSHGVPLRDMEFVQYHPTGLPGSGILMTEGCRGEGGILVNKNGYRYLQDYGMGPETPLGEPKNKYMELGPRDKVSQAFWHEWRKGNTIPTPRGDVVYLDLRHLGEKKLLERLPFICELAKAYVGVDPVKEPIPVRPTAHYTMGGIETDQQCETRIKGLFAVGECSSVGLHGANRLGSNSLAELVVFGRLAGEQAMQRAAQAGEANGAALDAQAADVEQRLKDLVNQEGNENWAKIRDEMGLSMEEGCGIYRTPELMQKTIDKLAELQERFKRVRITDNSSVFNTDLLYTIELGHGLNVAECMAHSAIARKESRGAHQRLDEGCTERDDVNFLKHTLAFREADGTTRLEYGDVKITTLPPAKRVYGAEADAAEKKETTHG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1.3.5.1

Gene Ontology (GO)

GO:0022900 A process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0009061 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.
GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
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:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways.
GO:0008177 Catalysis of the reaction: a quinone + succinate = a quinol + fumarate.
GO:0006113 The metabolic process that uses oxidation-reduction reactions of organic compounds and substrate-level phosphorylation for the generation of adenosine triphosphate (ATP), without consuming oxygen and is independent of electron transport chains.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

42 records

Show feature table

Start	End	DB	Term	Name
28	596	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
237	366	Gene3D	G3DSA:3.90.700.10	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
237	366	InterPro	IPR027477	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
8	18	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
543	577	Gene3D	G3DSA:4.10.80.40	succinate dehydrogenase protein domain
19	27	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	7	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
434	490	CDD	cd00167	SANT
434	490	InterPro	IPR001005	SANT/Myb domain
423	443	Coils	Coil	Coil
7	251	FunFam	G3DSA:3.50.50.60:FF:000017	Fumarate reductase flavoprotein subunit
543	577	FunFam	G3DSA:4.10.80.40:FF:000003	Fumarate reductase flavoprotein subunit
375	382	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
7	29	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
7	581	NCBIfam	TIGR01812	succinate dehydrogenase or fumarate reductase, flavoprotein subunit
7	581	InterPro	IPR014006	Succinate dehydrogenase/fumarate reductase, flavoprotein subunit
227	358	SUPERFAMILY	SSF56425	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
227	358	InterPro	IPR027477	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
7	397	Pfam	PF00890	FAD binding domain
7	397	InterPro	IPR003953	FAD-dependent oxidoreductase 2, FAD binding domain
2	416	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
2	416	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1	574	PIRSF	PIRSF000171	SDHA_APRA_LASPO
453	581	Pfam	PF02910	Fumarate reductase flavoprotein C-term
453	581	InterPro	IPR015939	Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal
43	52	ProSitePatterns	PS00504	Fumarate reductase / succinate dehydrogenase FAD-binding site.
43	52	InterPro	IPR003952	Fumarate reductase/succinate dehydrogenase, FAD-binding site
360	382	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
8	27	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
423	542	Gene3D	G3DSA:1.20.58.100	-
424	540	FunFam	G3DSA:1.20.58.100:FF:000001	Succinate dehydrogenase flavoprotein subunit (SdhA)
237	366	FunFam	G3DSA:3.90.700.10:FF:000003	Fumarate reductase flavoprotein subunit
473	493	Coils	Coil	Coil
5	575	PANTHER	PTHR11632	SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT
5	575	InterPro	IPR030664	FAD-dependent oxidoreductase SdhA/FrdA/AprA
444	590	SUPERFAMILY	SSF46977	Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain
444	590	InterPro	IPR037099	Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain superfamily
7	409	Gene3D	G3DSA:3.50.50.60	-
7	409	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1	27	Phobius	SIGNAL_PEPTIDE	Signal peptide region
3	582	NCBIfam	TIGR01176	fumarate reductase (quinol) flavoprotein subunit
3	582	InterPro	IPR005884	Fumarate reductase, flavoprotein subunit

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 #1

0.997

Likely same site as P2Rank 1 0.7 Å 37 shared residues 97% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #22

0.862

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Surrounding area

Site 3 FPocket #19

0.69

Likely same site as P2Rank 4 4.5 Å 18 shared residues 100% 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

0.975

Likely same site as FPocket 1 0.7 Å 37 shared residues 97% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.53

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Surrounding area

Site 3 P2Rank #3

0.511

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Surrounding area

Site 4 P2Rank #4

0.468

Likely same site as FPocket 19 4.5 Å 18 shared residues 100% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.085

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Surrounding area

Residue sets

UniProt: Active site:288-288 Proton acceptor

UniProt: Binding site:12-17

UniProt: Binding site:212-212

UniProt: Binding site:233-233

UniProt: Binding site:245-245

UniProt: Binding site:356-356

UniProt: Binding site:37-52

UniProt: Binding site:380-380

UniProt: Binding site:391-391

UniProt: Binding site:396-397

Binding pockets · FPocket

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

Site 1 FPocket #1

0.737

Likely same site as P2Rank 1 0.9 Å 41 shared residues 98% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #13

0.218

Likely same site as P2Rank 5 2.5 Å 15 shared residues 100% 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

0.983

Likely same site as FPocket 1 0.9 Å 41 shared residues 98% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.684

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Surrounding area

Site 3 P2Rank #3

0.595

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Surrounding area

Site 4 P2Rank #4

0.497

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Surrounding area

Site 5 P2Rank #5

0.098

Likely same site as FPocket 13 2.5 Å 15 shared residues 100% 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_A0A0H3GI02	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_31481	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.

86 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 36 records from similar proteins

Structural ligands 36 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3NP PDB via homolog 119.1 Da · LogP -0.26 · TPSA 80.4 Open detail RCSB PDB

3PE PDB via homolog Detail RCSB PDB

AT5 PDB via homolog Detail RCSB PDB

BOL PDB via homolog Detail RCSB PDB

BRS 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
3NP RCSB PDB	3P4S	P00363	119.1 Da LogP -0.26 TPSA 80.4	✓ Ro5	✓ Clean	`C(C[N+](=O)[O-])C(=O)O`
3PE RCSB PDB	6MYO	Q9YHT1	748.1 Da LogP 12.06 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN)OC…`
AT5 RCSB PDB	6MYS	Q9YHT1	366.2 Da LogP 2.79 TPSA 88.6	✓ Ro5	✓ Clean	`C[C@@H](C[C@H](C)C(=O)C1=C(C(=C(NC1=O)OC)OC)O)[…`
BOL RCSB PDB	3AED	Q0QF01	323.1 Da LogP 3.54 TPSA 29.1	✓ Ro5	✓ Clean	`c1ccc(cc1)NC(=O)c2ccccc2I`
BRS RCSB PDB	1KFY	P00363	322.7 Da LogP 4.01 TPSA 106.5	✓ Ro5	✓ Clean	`C[C@H](c1ccc(cc1)Cl)c2cc(cc(c2O)[N+](=O)[O-])[N…`
CBE RCSB PDB	2WDQ	P0AC41	235.3 Da LogP 2.62 TPSA 38.3	✓ Ro5	✓ Clean	`CC1=C(SCCO1)C(=O)Nc2ccccc2`
CDN RCSB PDB	1NEK	P0AC41	1151.5 Da LogP 14.77 TPSA 249.6	4 viol.	✓ Clean	`CCCCCCCCCCCCCCC(O)O[C@H](COC(CCCCC)O)CO[P@@](=O…`
CE1 RCSB PDB	1KF6	P00363	538.8 Da LogP 4.03 TPSA 94.1	1 viol.	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCOCCO`
DNT RCSB PDB	1NEN	P0AC41	282.3 Da LogP 3.89 TPSA 106.5	✓ Ro5	✓ Clean	`CCCCCC(C)c1cc(cc(c1O)[N+](=O)[O-])[N+](=O)[O-]`
EPH RCSB PDB	1NEK	P0AC41	709.9 Da LogP 10.16 TPSA 134.4	2 viol.	✓ Clean	`CCCC=CCC=CCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCC=CCC…`
F3S RCSB PDB	1KF6	P00363	295.8 Da LogP 2.59 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]2S[Fe]3[S]2[Fe]1S3`
F6A RCSB PDB	3ABV	Q0QF01	341.3 Da LogP 5.62 TPSA 29.1	1 viol.	✓ Clean	`c1ccc(cc1)c2cccc(c2)NC(=O)c3ccccc3C(F)(F)F`
F7A RCSB PDB	3AEB	Q0QF01	357.3 Da LogP 5.75 TPSA 38.3	1 viol.	✓ Clean	`c1ccc(cc1)Oc2cccc(c2)NC(=O)c3ccccc3C(F)(F)F`
F9A RCSB PDB	3AEA	Q0QF01	322.3 Da LogP 4.02 TPSA 32.3	✓ Ro5	✓ Clean	`CN(C)Cc1cccc(c1)NC(=O)c2ccccc2C(F)(F)F`
FD8 RCSB PDB	3AE9	Q0QF01	447.3 Da LogP 6.45 TPSA 38.3	1 viol.	✓ Clean	`c1ccc(c(c1)C(=O)Nc2cccc(c2)Oc3c(c(c(c(c3F)F)F)F…`
FES RCSB PDB	1KF6	P00363	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
FLC RCSB PDB	2B76	P00363	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
FTN RCSB PDB	6MYO	Q9YHT1	323.3 Da LogP 4.74 TPSA 38.3	✓ Ro5	✓ Clean	`CC(C)Oc1cccc(c1)NC(=O)c2ccccc2C(F)(F)F`
FUM RCSB PDB	3P4P	P00363	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)\C(=O)O`
GUA RCSB PDB	3P4R	P00363	132.1 Da LogP 0.33 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)CC(=O)O`
HQO RCSB PDB	1KF6	P00363	259.3 Da LogP 3.69 TPSA 47.2	✓ Ro5	Alert	`CCCCCCCc1cc(c2ccccc2[n+]1[O-])O`
LMT RCSB PDB	5XMJ	T2GB49	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…`
MLI RCSB PDB	6B58	P00363	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
MQ7 RCSB PDB	1L0V	P00363	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…`
MRN RCSB PDB	3AE5	Q0QF01	269.3 Da LogP 4.03 TPSA 38.3	✓ Ro5	✓ Clean	`Cc1ccccc1C(=O)Nc2cccc(c2)OC(C)C`
N1M RCSB PDB	3AE4	Q0QF01	261.1 Da LogP 1.65 TPSA 29.1	✓ Ro5	✓ Clean	`CNC(=O)c1ccccc1I`
OAA RCSB PDB	1KF6	P00363	131.1 Da LogP -2.22 TPSA 94.5	✓ Ro5	✓ Clean	`C(C(=O)C(=O)O)C(=O)[O-]`
PBF RCSB PDB	6B58	P00363	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`c1ccc(cc1)C(=O)c2ccc(cc2)C[C@@H](C(=O)O)N`
PCI RCSB PDB	3SFD	Q0QF01	266.3 Da LogP 4.66 TPSA 20.2	✓ Ro5	✓ Clean	`c1(c(c(c(c(c1Cl)Cl)Cl)Cl)Cl)O`
SLI RCSB PDB	3AE2	Q0QF01	213.2 Da LogP 2.64 TPSA 49.3	✓ Ro5	✓ Clean	`c1ccc(cc1)NC(=O)c2ccccc2O`
TEO RCSB PDB	2WDQ	P0AC41	132.1 Da LogP -3.14 TPSA 103.7	✓ Ro5	✓ Clean	`C(=C(\O)/[O-])\[C@H](C(=O)[O-])O`
TFZ RCSB PDB	3AE1	Q0QF01	265.2 Da LogP 3.96 TPSA 29.1	✓ Ro5	✓ Clean	`c1ccc(cc1)NC(=O)c2ccccc2C(F)(F)F`
TMG RCSB PDB	3SFE	Q0QF01	201.3 Da LogP 2.69 TPSA 41.6	✓ Ro5	✓ Clean	`c1ccc2c(c1)[nH]c(n2)c3cscn3`
TTF RCSB PDB	1ZP0	Q0QF01	222.2 Da LogP 2.45 TPSA 34.1	✓ Ro5	✓ Clean	`c1cc(sc1)C(=O)CC(=O)C(F)(F)F`
UMQ RCSB PDB	6MYO	Q9YHT1	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	1NEK	P0AC41	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`

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
ZINC100014200 ZINC	1.000	494.7 Da LogP 4.02 TPSA 84.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCO`
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…`
ZINC100070166 ZINC	1.000	290.4 Da LogP 3.17 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCO`
ZINC100310628 ZINC	1.000	478.7 Da LogP 4.78 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC100365196 ZINC	1.000	302.5 Da LogP 4.71 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCO`
ZINC101772322 ZINC	1.000	434.7 Da LogP 4.76 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC103600921 ZINC	1.000	466.7 Da LogP 3.24 TPSA 84.8	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1479 ZINC	1.000	323.3 Da LogP 4.74 TPSA 38.3	✓ Ro5	✓ Clean	`CC(C)Oc1cccc(NC(=O)c2ccccc2C(F)(F)F)c1`
ZINC14880431 ZINC	1.000	378.6 Da LogP 3.20 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC14881140 ZINC	1.000	306.4 Da LogP 2.41 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCOCCO`
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…`
ZINC1529471 ZINC	1.000	266.3 Da LogP 4.66 TPSA 20.2	✓ Ro5	✓ Clean	`Oc1c(Cl)c(Cl)c(Cl)c(Cl)c1Cl`
ZINC1529909 ZINC	1.000	259.3 Da LogP 3.69 TPSA 47.2	✓ Ro5	Alert	`CCCCCCCc1cc(O)c2ccccc2[n+]1[O-]`
ZINC16051619 ZINC	1.000	350.5 Da LogP 2.42 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCOCCOCCO`
ZINC173184 ZINC	1.000	261.1 Da LogP 1.65 TPSA 29.1	✓ Ro5	✓ Clean	`CNC(=O)c1ccccc1I`
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…`
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…`
ZINC2561081 ZINC	1.000	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O`
ZINC2561082 ZINC	1.000	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O`
ZINC2584424 ZINC	1.000	218.3 Da LogP 2.37 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCO`
ZINC43478 ZINC	1.000	235.3 Da LogP 2.62 TPSA 38.3	✓ Ro5	✓ Clean	`CC1=C(C(=O)Nc2ccccc2)SCCO1`
ZINC4521877 ZINC	1.000	234.3 Da LogP 1.61 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCOCCOCCOCCO`
ZINC5273610 ZINC	1.000	322.4 Da LogP 1.64 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCOCCOCCOCCOCCOCCO`
ZINC58538366 ZINC	1.000	392.6 Da LogP 3.59 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC58631420 ZINC	1.000	422.6 Da LogP 3.22 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
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@…`
ZINC59441819 ZINC	1.000	318.5 Da LogP 3.95 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCO`
ZINC59622400 ZINC	1.000	274.4 Da LogP 3.93 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCO`
ZINC61524 ZINC	1.000	323.1 Da LogP 3.54 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)c1ccccc1I`
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@…`
ZINC71788551 ZINC	1.000	334.5 Da LogP 3.19 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCO`
ZINC71788564 ZINC	1.000	262.4 Da LogP 2.39 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCO`
ZINC71788567 ZINC	1.000	406.6 Da LogP 3.98 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC73711 ZINC	1.000	201.3 Da LogP 2.69 TPSA 41.6	✓ Ro5	✓ Clean	`c1ccc2[nH]c(-c3cscn3)nc2c1`
ZINC8214594 ZINC	1.000	362.6 Da LogP 3.97 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCO`
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…`
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)…`
ZINC88260008 ZINC	1.000	390.6 Da LogP 4.75 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCO`
ZINC95784968 ZINC	1.000	450.7 Da LogP 4.00 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC95863931 ZINC	1.000	464.7 Da LogP 4.39 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`

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.