KpKP13 Protein target profile

oxidoreductase

Accession: KP13_02180

Gene: AHE42749.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GY52

Export view

Length 247

Pocket druggability (P2Rank · AlphaFold DB model) 0.95

Direct ligand evidence 0 76 total records

Functional annotation 0 EC 2 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: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.95, FPocket 0.77). 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 0.77. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.95. 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 (%): 38.983 Lower values reduce human off-target concern.
Human E-value: 1.19e-10
Gut microbiome similarity: 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 41.87 Higher values support similarity to known essential genes.
DEG E-value: 1.8700000000000002e-37 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.85 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.95

Structure A0A0H3GY52

Pocket Pocket 1

Druggability (FPocket) 0.77

Structure A0A0H3GY52

Pocket Pocket 7

ColabFold model

P2Rank 0.964 · Pocket 1

FPocket 0.821 · Pocket 15

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 108 / 4744 genomes with a hit

Prevalence 2.3%

Sequence

Primary amino-acid sequence viewer.

MGIALISGASRGIGRATALLLAQEGYTVAVNYHHNINAATEVVNTIVASGGKATALRADISDEAQVMAMFEAIDRMGEPLTALVNNAGILFTQCTVESLSAERINRVLATNVTGYFLCCREAVKRMSHRHGGKGGAIVNVSSAASRLGAPGEYVDYAASKGAVDTLTTGLALEVAAQGIRVNGVRPGLIYTEMHASGGEPGRVDRVKGSLPMQRGGQPEEVAQAIAWLLSDKASYVTGSFLELAGGK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

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:0016614 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group act as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
1	247	FunFam	G3DSA:3.40.50.720:FF:000173	3-oxoacyl-[acyl-carrier protein] reductase
143	171	ProSitePatterns	PS00061	Short-chain dehydrogenases/reductases family signature.
143	171	InterPro	IPR020904	Short-chain dehydrogenase/reductase, conserved site
8	246	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase
3	246	PANTHER	PTHR48107	NADPH-DEPENDENT ALDEHYDE REDUCTASE-LIKE PROTEIN, CHLOROPLASTIC-RELATED
211	231	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
211	231	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
129	145	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
129	145	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
3	20	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
3	20	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
156	175	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
156	175	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
78	89	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
78	89	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
177	194	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
177	194	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
3	246	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
3	246	InterPro	IPR036291	NAD(P)-binding domain superfamily
4	243	CDD	cd05233	SDR_c
135	143	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
135	143	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
78	89	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
156	175	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
2	246	Gene3D	G3DSA:3.40.50.720	-

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 · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.95

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.062

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.007

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #7

0.77

Show in viewer

Surrounding area

Pocket 2 FPocket #16

0.2

Show in viewer

Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.964

Likely same site as FPocket 1 0.7 Å 39 shared residues 95% of smaller site

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.055

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.007

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #15

0.821

Show in viewer

Surrounding area

Pocket 2 FPocket #1

0.581 Unusual size

Likely same site as P2Rank 1 0.7 Å 39 shared residues 95% of smaller site

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_A0A0H3GY52	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_02180	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.

76 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 26 records from similar proteins

Structural ligands 25 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2V4 PDB via homolog 338.3 Da · LogP 1.75 · TPSA 111.9 Open detail RCSB PDB

34X PDB via homolog Detail RCSB PDB

36E PDB via homolog Detail RCSB PDB

36G PDB via homolog Detail RCSB PDB

36I 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
2V4 RCSB PDB	4OSP	K0IB23	338.3 Da LogP 1.75 TPSA 111.9	✓ Ro5	Alert	`C[C@]1(Cc2cc(c3c(c2C(=O)C1)C(=O)c4cccc(c4C3=O)O…`
34X RCSB PDB	4BO8	O54438	311.3 Da LogP 3.05 TPSA 85.0	✓ Ro5	✓ Clean	`c1ccc(cc1)c2cn(c(n2)N)NC(=O)Nc3ccccc3F`
36E RCSB PDB	4BNT	O54438	186.1 Da LogP 2.58 TPSA 28.7	✓ Ro5	✓ Clean	`c1ccc2c(c1)[nH]c(n2)C(F)(F)F`
36G RCSB PDB	4BO4	O54438	282.3 Da LogP 3.68 TPSA 41.6	✓ Ro5	✓ Clean	`COc1ccccc1NC(=O)N2CCCc3c2cccc3`
36I RCSB PDB	4BNY	O54438	297.4 Da LogP 3.19 TPSA 38.2	✓ Ro5	✓ Clean	`c1ccc(cc1)c2nc3ccsc3c(n2)N4CCOCC4`
36K RCSB PDB	4BO2	O54438	310.4 Da LogP 3.71 TPSA 68.2	✓ Ro5	✓ Clean	`CCn1c2ccccc2nc1NC(=O)Nc3ccccc3OC`
36P RCSB PDB	4BO6	O54438	312.4 Da LogP 4.07 TPSA 33.2	✓ Ro5	✓ Clean	`c1ccc2c(c1)CCN2C(=O)c3csc(n3)c4ccsc4`
3X3 RCSB PDB	4BO9	O54438	318.3 Da LogP 3.50 TPSA 66.0	✓ Ro5	✓ Clean	`c1ccc(cc1)n2nc(nn2)c3ccccc3OCc4ccco4`
8M5 RCSB PDB	4BNZ	O54438	250.3 Da LogP 3.43 TPSA 34.0	✓ Ro5	✓ Clean	`Cn1cc(c2c1cccc2)C(=O)Nc3ccccc3`
9KQ RCSB PDB	4BNU	O54438	273.3 Da LogP 2.88 TPSA 56.5	✓ Ro5	✓ Clean	`c1ccc(cc1)c2nc3ccccc3c(n2)n4cnnc4`
CAC RCSB PDB	3I3O	A0A6L8PL20	137.0 Da LogP -0.52 TPSA 40.1	✓ Ro5	✓ Clean	`C[As](=O)(C)[O-]`
CUE RCSB PDB	3QWI	O93874	268.2 Da LogP 3.10 TPSA 83.8	✓ Ro5	✓ Clean	`c1cc2c(cc1O)oc-3c2C(=O)Oc4c3ccc(c4)O`
FXE RCSB PDB	4BO0	O54438	326.4 Da LogP 3.23 TPSA 77.4	✓ Ro5	✓ Clean	`Cn1c2cccc(c2c(n1)NC(=O)Nc3ccccc3OC)OC`
GEN RCSB PDB	4FJ1	O93874	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`c1cc(ccc1C2=COc3cc(cc(c3C2=O)O)O)O`
HHF RCSB PDB	4FJ0	O93874	254.2 Da LogP 2.87 TPSA 70.7	✓ Ro5	✓ Clean	`c1ccc(cc1)C2=C(C(=O)c3ccc(cc3O2)O)O`
J2T RCSB PDB	4BO7	O54438	252.3 Da LogP 1.75 TPSA 68.0	✓ Ro5	✓ Clean	`c1cc2c(cc1Nc3ccc4nnnn4n3)CCC2`
KMP RCSB PDB	3QWH	O93874	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	✓ Clean	`c1cc(ccc1C2=C(C(=O)c3c(cc(cc3O2)O)O)O)O`
MLH RCSB PDB	6T65	V5VHN7	417.3 Da LogP 4.34 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c2cc(c(cc2n(c1CN(C)C)c3ccccc3)Br)O`
NAE RCSB PDB	3I3O	A0A6L8PL20	719.5 Da LogP -3.52 TPSA 338.2	3 viol.	✓ Clean	`CC(=O)Cc1cc[n+](cc1C(=O)N)[C@H]2[C@@H]([C@@H]([…`
NKH RCSB PDB	4BO1	O54438	342.8 Da LogP 4.16 TPSA 60.5	✓ Ro5	✓ Clean	`COc1cc(c(cc1Cl)OC)NC(=O)c2cccc3c2nccc3`
O74 RCSB PDB	4BNX	O54438	347.8 Da LogP 4.53 TPSA 53.5	✓ Ro5	✓ Clean	`c1ccc2c(c1)C(=N/C(=C/3\C=CC=CC3=O)/N2)Nc4ccccc4…`
Q7U RCSB PDB	4BNV	O54438	300.7 Da LogP 3.87 TPSA 59.0	✓ Ro5	✓ Clean	`Cn1c2ccccc2nc1NC(=O)Nc3ccccc3Cl`
QSO RCSB PDB	4FJ2	O93874	284.3 Da LogP 2.88 TPSA 79.9	✓ Ro5	✓ Clean	`COc1ccc(cc1)C2=COc3cc(cc(c3C2=O)O)O`
U98 RCSB PDB	4BO3	O54438	317.3 Da LogP 2.49 TPSA 85.1	✓ Ro5	✓ Clean	`c1cc(cc(c1)Nc2c(cccn2)S(=O)(=O)N)C(F)(F)F`
WI4 RCSB PDB	4BO5	O54438	271.7 Da LogP 3.06 TPSA 55.6	✓ Ro5	✓ Clean	`c1ccc(c(c1)Nc2ncnc(n2)n3cccc3)Cl`

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

No ChEMBL bioactivity data found for this exact protein.

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

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL361197 ChEMBL	O93874	6.16 ~691.8 nM	238.3 Da LogP 3.44 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccccc1)OCc1ccccc1`

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
ZINC1219 ZINC	1.000	268.2 Da LogP 3.10 TPSA 83.8	✓ Ro5	✓ Clean	`O=c1oc2cc(O)ccc2c2oc3cc(O)ccc3c12`
ZINC1233995 ZINC	1.000	417.3 Da LogP 4.34 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccccc2)c2cc(Br)c(O)cc12`
ZINC12358883 ZINC	1.000	238.3 Da LogP 3.44 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccccc1)OCc1ccccc1`
ZINC13152723 ZINC	1.000	310.4 Da LogP 3.71 TPSA 68.2	✓ Ro5	✓ Clean	`CCn1c(NC(=O)Nc2ccccc2OC)nc2ccccc21`
ZINC1399281 ZINC	1.000	297.4 Da LogP 3.19 TPSA 38.2	✓ Ro5	✓ Clean	`c1ccc(-c2nc(N3CCOCC3)c3sccc3n2)cc1`
ZINC1857742182 ZINC	1.000	238.3 Da LogP 3.44 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(C=Cc1ccccc1)OCc1ccccc1`
ZINC18825330 ZINC	1.000	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(-c2ccc(O)cc2)coc2cc(O)cc(O)c12`
ZINC18847037 ZINC	1.000	284.3 Da LogP 2.88 TPSA 79.9	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(O)cc(O)c3c2=O)cc1`
ZINC27923853 ZINC	1.000	300.7 Da LogP 3.87 TPSA 59.0	✓ Ro5	✓ Clean	`Cn1c(NC(=O)Nc2ccccc2Cl)nc2ccccc21`
ZINC318945 ZINC	1.000	282.3 Da LogP 3.68 TPSA 41.6	✓ Ro5	✓ Clean	`COc1ccccc1NC(=O)N1CCCc2ccccc21`
ZINC3869768 ZINC	1.000	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccc(O)cc2)oc2cc(O)cc(O)c12`
ZINC4654730 ZINC	1.000	338.3 Da LogP 1.75 TPSA 111.9	✓ Ro5	Alert	`C[C@]1(O)CC(=O)c2c(cc(O)c3c2C(=O)c2cccc(O)c2C3=…`
ZINC4803379 ZINC	1.000	238.3 Da LogP 3.44 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C\c1ccccc1)OCc1ccccc1`
ZINC481463 ZINC	1.000	317.3 Da LogP 2.49 TPSA 85.1	✓ Ro5	✓ Clean	`NS(=O)(=O)c1cccnc1Nc1cccc(C(F)(F)F)c1`
ZINC6032158 ZINC	1.000	338.3 Da LogP 1.75 TPSA 111.9	✓ Ro5	Alert	`C[C@@]1(O)CC(=O)c2c(cc(O)c3c2C(=O)c2cccc(O)c2C3…`
ZINC6116596 ZINC	1.000	254.2 Da LogP 2.87 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccccc2)oc2cc(O)ccc12`
ZINC7913991 ZINC	1.000	250.3 Da LogP 3.43 TPSA 34.0	✓ Ro5	✓ Clean	`Cn1cc(C(=O)Nc2ccccc2)c2ccccc21`
ZINC8231765 ZINC	1.000	342.8 Da LogP 4.16 TPSA 60.5	✓ Ro5	✓ Clean	`COc1cc(NC(=O)c2cccc3cccnc23)c(OC)cc1Cl`
ZINC8429509 ZINC	1.000	312.4 Da LogP 4.07 TPSA 33.2	✓ Ro5	✓ Clean	`O=C(c1csc(-c2ccsc2)n1)N1CCc2ccccc21`
ZINC8723457 ZINC	1.000	252.3 Da LogP 1.75 TPSA 68.0	✓ Ro5	✓ Clean	`c1cc2c(cc1Nc1ccc3nnnn3n1)CCC2`
ZINC8726387 ZINC	1.000	273.3 Da LogP 2.88 TPSA 56.5	✓ Ro5	✓ Clean	`c1ccc(-c2nc(-n3cnnc3)c3ccccc3n2)cc1`
ZINC89647 ZINC	1.000	271.7 Da LogP 3.06 TPSA 55.6	✓ Ro5	✓ Clean	`Clc1ccccc1Nc1ncnc(-n2cccc2)n1`
ZINC9338279 ZINC	1.000	311.3 Da LogP 3.05 TPSA 85.0	✓ Ro5	✓ Clean	`Nc1nc(-c2ccccc2)cn1NC(=O)Nc1ccccc1F`
ZINC6018481 ZINC	0.875	298.3 Da LogP 3.18 TPSA 68.9	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(OC)cc(O)c3c2=O)cc1`
ZINC451821 ZINC	0.857	268.3 Da LogP 3.29 TPSA 41.6	✓ Ro5	✓ Clean	`COc1ccccc1NC(=O)N1CCc2ccccc21`
ZINC8453886 ZINC	0.849	431.3 Da LogP 4.65 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccc(C)cc2)c2cc(Br)c(O)c…`
ZINC14504998 ZINC	0.844	254.3 Da LogP 3.15 TPSA 46.5	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccc(O)cc1)OCc1ccccc1`
ZINC39203780 ZINC	0.844	268.2 Da LogP 3.10 TPSA 83.8	✓ Ro5	✓ Clean	`O=c1oc2cc(O)ccc2c2oc3ccc(O)cc3c12`
ZINC12534489 ZINC	0.833	307.4 Da LogP 3.39 TPSA 63.1	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(NC(=O)c2cn(C)c3ccccc23)cc1`
ZINC27923895 ZINC	0.833	335.2 Da LogP 4.52 TPSA 59.0	✓ Ro5	✓ Clean	`Cn1c(NC(=O)Nc2cccc(Cl)c2Cl)nc2ccccc21`
ZINC7917230 ZINC	0.833	264.3 Da LogP 3.74 TPSA 34.0	✓ Ro5	✓ Clean	`Cc1ccc(NC(=O)c2cn(C)c3ccccc23)cc1`
ZINC6093351 ZINC	0.824	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccc(O)cc2)oc2cc(O)ccc12`
ZINC304562 ZINC	0.811	333.1 Da LogP 3.63 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(-c2ccc(Br)cc2)coc2cc(O)cc(O)c12`
ZINC32497089 ZINC	0.811	278.3 Da LogP 2.79 TPSA 51.1	✓ Ro5	✓ Clean	`Cn1cc(C(=O)Nc2ccccc2)c(=O)c2ccccc21`
ZINC5731170 ZINC	0.811	288.7 Da LogP 3.52 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(-c2ccc(Cl)cc2)coc2cc(O)cc(O)c12`
ZINC5997152 ZINC	0.811	272.2 Da LogP 3.01 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(-c2ccc(F)cc2)coc2cc(O)cc(O)c12`
ZINC120273 ZINC	0.806	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccccc2)oc2cc(O)cc(O)c12`
ZINC2149675 ZINC	0.806	254.2 Da LogP 2.87 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(-c2ccccc2)coc2cc(O)cc(O)c12`
ZINC57845 ZINC	0.806	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2cccc(O)c2)oc2cc(O)ccc12`
ZINC27923339 ZINC	0.800	340.4 Da LogP 3.72 TPSA 77.4	✓ Ro5	✓ Clean	`CCn1c(NC(=O)Nc2cc(OC)ccc2OC)nc2ccccc21`
ZINC5222178 ZINC	0.800	431.3 Da LogP 4.64 TPSA 43.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccccc2)c2cc(Br)c(OC)cc12`
ZINC95453238 ZINC	0.800	360.8 Da LogP 4.30 TPSA 60.5	✓ Ro5	✓ Clean	`COc1cc(NC(=O)c2cc(F)cc3cccnc23)c(OC)cc1Cl`
ZINC8074404 ZINC	0.795	293.3 Da LogP 2.53 TPSA 77.1	✓ Ro5	✓ Clean	`Cn1cc(C(=O)Nc2ccc(C(N)=O)cc2)c2ccccc21`
ZINC2888441 ZINC	0.794	272.7 Da LogP 4.10 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccccc1)OCc1ccc(Cl)cc1`
ZINC3103992 ZINC	0.794	272.7 Da LogP 4.10 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccc(Cl)cc1)OCc1ccccc1`
ZINC3228605 ZINC	0.794	256.3 Da LogP 3.58 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccc(F)cc1)OCc1ccccc1`
ZINC11865148 ZINC	0.791	282.3 Da LogP 3.48 TPSA 59.7	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(O)cc(C)c3c2=O)cc1`
ZINC14811807 ZINC	0.791	298.3 Da LogP 3.18 TPSA 68.9	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(O)cc(OC)c3c2=O)cc1`
ZINC32726013 ZINC	0.789	251.3 Da LogP 2.83 TPSA 46.9	✓ Ro5	✓ Clean	`Cn1cc(C(=O)Nc2ccncc2)c2ccccc21`
ZINC15934558 ZINC	0.787	312.4 Da LogP 3.69 TPSA 50.8	✓ Ro5	✓ Clean	`COc1ccc(OC)c(NC(=O)N2CCCc3ccccc32)c1`

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.

Cross-references

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

Sequence

UniProt A0A0H3GY52

Chemistry

ChEMBL CHEMBL361197