Protein target profile

KP13_03279

Succinate dehydrogenase flavoprotein subunit

Genome: KpKP13 Gene: AHE45658.1 sdhA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GU54

Export view

Length 588

Pocket druggability 0.582

Direct ligand evidence 0 91 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.58. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.97. Structure available AlphaFold DB model + ColabFold model 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 (%): 63.514 Lower values reduce human off-target concern.
Human E-value: 1.69e-120
Gut microbiome similarity: 3.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 97.449 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: 98.44 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 0.582

Structure A0A0H3GU54

Pocket Pocket 27

P2Rank 0.968

Structure A0A0H3GU54

Pocket Pocket 1

ColabFold model

FPocket 0.895 · Pocket 1

P2Rank 0.977 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 177 / 4744 genomes with a hit

Prevalence 3.7%

Cross-references

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

Sequence

UniProt A0A0H3GU54

Sequence

Primary amino-acid sequence viewer.

MKLPVREFDAVVIGAGGAGMRAALQISQSGQTCALLSKVFPTRSHTVSAQGGITVALGNSHEDNWEWHMYDTVKGSDYIGDQDAIEYMCKTGPEAILELEHMGLPFSRLDDGRIYQRPFGGQSKNFGGEQAARTAAAADRTGHALLHTLYQQNLKNHTTIFSEWYALDLVKNQDGAVVGCTALCIETGEVVYFKARATVLATGGAGRIYQSTTNAHINTGDGVGMAIRAGVPVQDMEMWQFHPTGIAGAGVLVTEGCRGEGGYLLNKHGERFMERYAPNAKDLAGRDVVARSIMIEIREGRGCDGPWGPHAKLKLDHLGKEVLESRLPGILELSRTFAHVDPVKEPIPVIPTCHYMMGGIPTKVTGQALTVNEKGEDVVIPGLFAVGEIACVSVHGANRLGGNSLLDLVVFGRAAGLHLQESIAEQGTLRDASESDIEGSLDRLNRWNNTRSGEDPVAIRKALQECMQHNFSVFREGDAMHKGLEQLKVIRERLKNARLDDTSSEFNTQRVECLELDNLMETAYATAVSANFRTESRGAHSRFDFPDRDDENWLCHSLYLPESESMTRRSVNMEPKLRPAFPPKIRTY

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: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:0006099 A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.
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: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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

30 records

Show feature table

Start	End	DB	Term	Name
1	579	PIRSF	PIRSF000171	SDHA_APRA_LASPO
246	350	Gene3D	G3DSA:3.90.700.10	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
246	350	InterPro	IPR027477	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
548	588	FunFam	G3DSA:4.10.80.40:FF:000001	Succinate dehydrogenase flavoprotein subunit
452	588	SUPERFAMILY	SSF46977	Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain
452	588	InterPro	IPR037099	Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain superfamily
43	52	ProSitePatterns	PS00504	Fumarate reductase / succinate dehydrogenase FAD-binding site.
43	52	InterPro	IPR003952	Fumarate reductase/succinate dehydrogenase, FAD-binding site
246	350	FunFam	G3DSA:3.90.700.10:FF:000001	Mitochondrial succinate dehydrogenase flavoprotein subunit
548	588	Gene3D	G3DSA:4.10.80.40	succinate dehydrogenase protein domain
431	547	Gene3D	G3DSA:1.20.58.100	-
9	416	Gene3D	G3DSA:3.50.50.60	-
9	416	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
6	588	PANTHER	PTHR11632	SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT
6	588	InterPro	IPR030664	FAD-dependent oxidoreductase SdhA/FrdA/AprA
236	356	SUPERFAMILY	SSF56425	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
236	356	InterPro	IPR027477	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
460	588	Pfam	PF02910	Fumarate reductase flavoprotein C-term
460	588	InterPro	IPR015939	Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal
9	588	NCBIfam	TIGR01812	succinate dehydrogenase or fumarate reductase, flavoprotein subunit
9	588	InterPro	IPR014006	Succinate dehydrogenase/fumarate reductase, flavoprotein subunit
4	439	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
4	439	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
9	405	Pfam	PF00890	FAD binding domain
9	405	InterPro	IPR003953	FAD-dependent oxidoreductase 2, FAD binding domain
6	588	NCBIfam	TIGR01816	succinate dehydrogenase flavoprotein subunit
6	588	InterPro	IPR011281	Succinate dehydrogenase, flavoprotein subunit
431	547	FunFam	G3DSA:1.20.58.100:FF:000001	Succinate dehydrogenase flavoprotein subunit (SdhA)
10	29	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
368	390	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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 #27

0.582

Show in viewer

Surrounding area

Site 2 FPocket #16

0.37

Show in viewer

Surrounding area

Site 3 FPocket #29

0.216

Likely same site as P2Rank 2 7.4 Å 10 shared residues 67% of smaller site

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.968

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.448

Likely same site as FPocket 29 7.4 Å 10 shared residues 67% of smaller site

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.376

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.227

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.154

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:248-248 Proton acceptor

UniProt: Binding site:183-183

UniProt: Binding site:204-204

UniProt: Binding site:216-216

UniProt: Binding site:316-316

UniProt: Binding site:350-350

UniProt: Binding site:361-361

UniProt: Binding site:366-367

Binding pockets · FPocket

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

Site 1 FPocket #1

0.895

Likely same site as P2Rank 1 1.3 Å 43 shared residues 100% of smaller site

Unusual size

Show in viewer

Surrounding area

Site 2 FPocket #12

0.421

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.977

Likely same site as FPocket 1 1.3 Å 43 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.293

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.209

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.154

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.114

Show in viewer

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_A0A0H3GU54	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03279	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.

91 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 41 records from similar proteins

Structural ligands 41 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

12J PDB via homolog 381.2 Da · LogP 4.33 · TPSA 38.3 Open detail RCSB PDB

3NP PDB via homolog Detail RCSB PDB

3PE PDB via homolog Detail RCSB PDB

4YP PDB via homolog Detail RCSB PDB

AT5 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
12J RCSB PDB	4YSZ	Q33862	381.2 Da LogP 4.33 TPSA 38.3	✓ Ro5	✓ Clean	`CC(C)Oc1cccc(c1)NC(=O)c2ccccc2I`
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…`
4YP RCSB PDB	5C2T	Q33862	303.4 Da LogP 3.35 TPSA 69.4	✓ Ro5	Alert	`CC1=C(C(=O)C(=C(C1=O)N)OC)C/C=C(\C)/CCC=C(C)C`
AT5 RCSB PDB	2ACZ	P0AC41	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-]`
E23 RCSB PDB	4YSX	Q33862	335.4 Da LogP 4.93 TPSA 29.1	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(cc1)CNC(=O)c2ccccc2C(F)(F)F`
E24 RCSB PDB	4YSY	Q33862	348.2 Da LogP 4.94 TPSA 29.1	✓ Ro5	✓ Clean	`c1ccc(c(c1)C(=O)NCc2ccc(cc2Cl)Cl)C(F)(F)F`
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	1NEK	P0AC41	295.8 Da LogP 2.59 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]2S[Fe]3[S]2[Fe]1S3`
F6A RCSB PDB	4YTM	Q33862	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	4YTN	Q33862	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	1NEK	P0AC41	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	3VRB	Q33862	323.3 Da LogP 4.74 TPSA 38.3	✓ Ro5	✓ Clean	`CC(C)Oc1cccc(c1)NC(=O)c2ccccc2C(F)(F)F`
FUM RCSB PDB	3VRB	Q33862	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`
MLI RCSB PDB	3VRA	Q33862	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	4YT0	Q33862	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	1NEK	P0AC41	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	2WDR	P0AC41	266.3 Da LogP 4.66 TPSA 20.2	✓ Ro5	✓ Clean	`c1(c(c(c(c(c1Cl)Cl)Cl)Cl)Cl)O`
RQX RCSB PDB	3VR8	Q33862	263.3 Da LogP 2.41 TPSA 69.4	✓ Ro5	Alert	`CCC/C(=C/CC1=C(C(=O)C(=C(C1=O)OC)N)C)/C`
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)…`
UQ1 RCSB PDB	5C3J	Q33862	250.3 Da LogP 2.32 TPSA 52.6	✓ Ro5	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)CC=C(C)C`
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`
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`
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-]`
ZINC1532641 ZINC	1.000	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`
ZINC16051619 ZINC	1.000	350.5 Da LogP 2.42 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCOCCOCCO`
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…`
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`
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`
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](…`
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@…`
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.