KpKP13 Protein target profile

Histidine biosynthesis bifunctional protein

Accession: KP13_03770

Gene: hisB AHE43693.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GV71

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Length 355

Pocket druggability (P2Rank · AlphaFold DB model) 0.13

Direct ligand evidence 0 54 total records

Functional annotation 0 EC 6 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Risks to review

Microbiome similarity 177 of 4744 screened genomes (3.7%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.32. Weak second pocket-predictor signal P2Rank predicted binding-site probability 0.13.

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: No hit
Gut microbiome similarity: 3.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 60.497 Higher values support similarity to known essential genes.
DEG E-value: 5.1e-165 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 95.33 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) 0.13

Structure A0A0H3GV71

Pocket Pocket 1

Druggability (FPocket) 0.318

Structure A0A0H3GV71

Pocket Pocket 4

ColabFold model

P2Rank 0.231 · Pocket 1

FPocket 0.846 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 177 / 4744 genomes with a hit

Prevalence 3.7%

Sequence

Primary amino-acid sequence viewer.

MTQKYLFIDRDGTLISEPPEDFQVDRFDKLAFEPQVIPALLKLQQEGYKLVMITNQDGLGTDSLPQEAFDGPHNLMMQIFASQCVNFEEVLICPHFPGDNCACRKPKTQLVLPWLEEGVLDKSHSYVIGDRATDLELADNMGITGLRYDRETLDWPTICEQLTRRDRYAHVERVTKETQVDVKVWLDREGGSKIHTGVGFFDHMLDQIATHGGFRMEVNVGGDLYIDDHHTVEDTGLALGEALKLALGDKRGINRFGFVLPMDECLARCALDISGRPHLEYKADFTYQRVGDLSTEMVEHFFRSLSYTMAVTLHLKTKGKNDHHRVESLFKAFGRTLRQAIRVQGDALPSSKGVL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
GO:0004424 Catalysis of the reaction: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O.
GO:0016791 Catalysis of the hydrolysis of a phosphoric monoester, releasing a phosphate.
GO:0004401 Catalysis of the reaction: L-histidinol phosphate + H2O = L-histidinol + phosphate.
GO:0046872 Binding to a metal ion.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

37 records

Show feature table

Start	End	DB	Term	Name
160	355	PANTHER	PTHR23133	IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE HIS7
160	355	InterPro	IPR000807	Imidazoleglycerol-phosphate dehydratase
4	147	NCBIfam	TIGR01662	HAD-IIIA family hydrolase
4	147	InterPro	IPR006549	HAD-superfamily hydrolase,subfamily IIIA
226	239	ProSitePatterns	PS00954	Imidazoleglycerol-phosphate dehydratase signature 1.
226	239	InterPro	IPR020565	Imidazoleglycerol-phosphate dehydratase, conserved site
5	144	NCBIfam	TIGR01656	histidinol-phosphate phosphatase domain
5	144	InterPro	IPR006543	Histidinol-phosphate phosphatase
319	331	ProSitePatterns	PS00955	Imidazoleglycerol-phosphate dehydratase signature 2.
319	331	InterPro	IPR020565	Imidazoleglycerol-phosphate dehydratase, conserved site
162	254	Gene3D	G3DSA:3.30.230.40	Imidazole glycerol phosphate dehydratase; domain 1
162	254	InterPro	IPR038494	Imidazole glycerol phosphate dehydratase domain superfamily
1	162	FunFam	G3DSA:3.40.50.1000:FF:000061	Histidine biosynthesis bifunctional protein HisB
167	355	Hamap	MF_00076	Imidazoleglycerol-phosphate dehydratase [hisB].
167	355	InterPro	IPR000807	Imidazoleglycerol-phosphate dehydratase
1	161	Gene3D	G3DSA:3.40.50.1000	-
1	161	InterPro	IPR023214	HAD superfamily
2	355	Hamap	MF_01022	Histidine biosynthesis bifunctional protein HisB [hisB].
2	355	InterPro	IPR020566	Histidine biosynthesis bifunctional protein HisB
103	145	Pfam	PF13242	HAD-hyrolase-like
4	148	CDD	cd07503	HAD_HisB-N
167	251	SUPERFAMILY	SSF54211	Ribosomal protein S5 domain 2-like
167	251	InterPro	IPR020568	Ribosomal protein S5 domain 2-type fold
255	355	Gene3D	G3DSA:3.30.230.40	Imidazole glycerol phosphate dehydratase; domain 1
255	355	InterPro	IPR038494	Imidazole glycerol phosphate dehydratase domain superfamily
3	162	NCBIfam	TIGR01261	HisB N-terminal histidinol-phosphatase domain
3	162	InterPro	IPR005954	Histidine biosynthesis bifunctional protein, N-terminal histidinol-phosphatase domain
255	355	FunFam	G3DSA:3.30.230.40:FF:000001	Imidazoleglycerol-phosphate dehydratase HisB
169	355	CDD	cd07914	IGPD
169	355	InterPro	IPR000807	Imidazoleglycerol-phosphate dehydratase
196	337	Pfam	PF00475	Imidazoleglycerol-phosphate dehydratase
196	337	InterPro	IPR000807	Imidazoleglycerol-phosphate dehydratase
160	254	FunFam	G3DSA:3.30.230.40:FF:000003	Imidazoleglycerol-phosphate dehydratase HisB
1	156	SUPERFAMILY	SSF56784	HAD-like
1	156	InterPro	IPR036412	HAD-like superfamily
252	342	SUPERFAMILY	SSF54211	Ribosomal protein S5 domain 2-like
252	342	InterPro	IPR020568	Ribosomal protein S5 domain 2-type fold

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 · P2Rank

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

Pocket 1 P2Rank #1

0.13

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Surrounding area

Pocket 2 P2Rank #2

0.009

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #4

0.318

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:11-11 Proton donor

UniProt: Active site:9-9 Nucleophile

UniProt: Binding site:101-101

UniProt: Binding site:103-103

UniProt: Binding site:11-11

UniProt: Binding site:130-130

UniProt: Binding site:9-9

UniProt: Binding site:93-93

UniProt: Binding site:95-95

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_A0A0H3GV71	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03770	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.

54 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 20 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 15 direct and transferred ChEMBL records

Proposed compounds 34 similarity-based ZINC candidates

Best available ligand signal

5DL PDB via homolog 207.1 Da · LogP -1.18 · TPSA 108.5 Open detail RCSB PDB

5LD PDB via homolog Detail RCSB PDB

EMC PDB via homolog Detail RCSB PDB

IYP PDB via homolog Detail RCSB PDB

TRI 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
5DL RCSB PDB	5EKW	O23346	207.1 Da LogP -1.18 TPSA 108.5	✓ Ro5	✓ Clean	`c1ncn(n1)C[C@@H](CP(=O)(O)O)O`
5LD RCSB PDB	6FWH	L8H477	207.1 Da LogP -1.18 TPSA 108.5	✓ Ro5	✓ Clean	`c1ncn(n1)C[C@H](CP(=O)(O)O)O`
EMC RCSB PDB	1RHY	P0CO22	229.7 Da LogP 0.97 TPSA 0.0	✓ Ro5	✓ Clean	`CC[Hg+]`
IYP RCSB PDB	4MU4	O23346	238.1 Da LogP -1.09 TPSA 135.9	✓ Ro5	✓ Clean	`c1c([nH]cn1)[C@@H]([C@@H](COP(=O)(O)O)O)O`
TRI RCSB PDB	4MU0	O23346	69.1 Da LogP -0.20 TPSA 41.6	✓ Ro5	✓ Clean	`c1[nH]cnn1`

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
CHEMBL50542 ChEMBL	P0CO23	9.22 ~0.6 nM	207.1 Da LogP -1.18 TPSA 108.5	✓ Ro5	✓ Clean	`O=P(O)(O)CC(O)Cn1cncn1`
CHEMBL63035 ChEMBL	P0CO23	7.82 ~15.1 nM	206.1 Da LogP -1.22 TPSA 114.3	✓ Ro5	✓ Clean	`NC(Cn1cncn1)CP(=O)(O)O`
CHEMBL60155 ChEMBL	P0CO23	7.10 ~79.4 nM	340.3 Da LogP 0.02 TPSA 126.6	✓ Ro5	✓ Clean	`O=C(COc1ccccc1)NC(Cn1cncn1)CP(=O)(O)O`
CHEMBL303762 ChEMBL	P0CO23	6.64 ~229.1 nM	264.2 Da LogP -2.07 TPSA 137.6	✓ Ro5	✓ Clean	`O=C(CO)NC(Cn1cncn1)CP(=O)(O)O`
CHEMBL418642 ChEMBL	P0CO23	6.64 ~229.1 nM	354.3 Da LogP 0.41 TPSA 126.6	✓ Ro5	✓ Clean	`CC(Oc1ccccc1)C(=O)NC(Cn1cncn1)CP(=O)(O)O`
CHEMBL62933 ChEMBL	P0CO23	6.60 ~251.2 nM	356.3 Da LogP 0.73 TPSA 117.3	✓ Ro5	✓ Clean	`O=C(CSc1ccccc1)NC(Cn1cncn1)CP(=O)(O)O`
CHEMBL423851 ChEMBL	P0CO23	6.57 ~269.2 nM	338.3 Da LogP 0.57 TPSA 117.3	✓ Ro5	✓ Clean	`O=C(CCc1ccccc1)NC(Cn1cncn1)CP(=O)(O)O`
CHEMBL64769 ChEMBL	P0CO23	6.47 ~338.8 nM	304.3 Da LogP 0.52 TPSA 117.3	✓ Ro5	✓ Clean	`CCCCCC(=O)NC(Cn1cncn1)CP(=O)(O)O`
CHEMBL66416 ChEMBL	P0CO23	6.47 ~338.8 nM	324.3 Da LogP 0.18 TPSA 117.3	✓ Ro5	✓ Clean	`O=C(Cc1ccccc1)NC(Cn1cncn1)CP(=O)(O)O`
CHEMBL304038 ChEMBL	P0CO23	6.26 ~549.5 nM	374.7 Da LogP 0.67 TPSA 126.6	✓ Ro5	✓ Clean	`O=C(COc1ccc(Cl)cc1)NC(Cn1cncn1)CP(=O)(O)O`
CHEMBL63147 ChEMBL	P0CO23	6.25 ~562.3 nM	330.3 Da LogP 0.24 TPSA 117.3	✓ Ro5	✓ Clean	`O=C(Cc1cccs1)NC(Cn1cncn1)CP(=O)(O)O`
CHEMBL65577 ChEMBL	P0CO23	6.16 ~691.8 nM	334.3 Da LogP -0.72 TPSA 143.6	✓ Ro5	✓ Clean	`COC(=O)CCCC(=O)NC(Cn1cncn1)CP(=O)(O)O`
CHEMBL293612 ChEMBL	P0CO23	6.10 ~794.3 nM	248.2 Da LogP -1.04 TPSA 117.3	✓ Ro5	✓ Clean	`CC(=O)NC(Cn1cncn1)CP(=O)(O)O`
CHEMBL294077 ChEMBL	P0CO23	6.10 ~794.3 nM	380.4 Da LogP 0.92 TPSA 117.3	✓ Ro5	✓ Clean	`CC1(CCC(=O)NC(Cn2cncn2)CP(=O)(O)O)SCCS1`
CHEMBL294774 ChEMBL	P0CO23	6.06 ~871.0 nM	330.3 Da LogP 0.91 TPSA 117.3	✓ Ro5	✓ Clean	`O=C(CCC1CCCC1)NC(Cn1cncn1)CP(=O)(O)O`

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
ZINC3869788 ZINC	1.000	238.1 Da LogP -1.09 TPSA 135.9	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H](O)[C@@H](O)c1cnc[nH]1`
ZINC585150369 ZINC	0.576	304.3 Da LogP 0.88 TPSA 78.3	✓ Ro5	✓ Clean	`C[C@@H](Oc1ccccc1)C(=O)NCCOCCn1cncn1`
ZINC585150371 ZINC	0.576	304.3 Da LogP 0.88 TPSA 78.3	✓ Ro5	✓ Clean	`C[C@H](Oc1ccccc1)C(=O)NCCOCCn1cncn1`
ZINC58481767 ZINC	0.567	336.4 Da LogP 2.41 TPSA 69.0	✓ Ro5	✓ Clean	`C[C@H](Oc1ccccc1)C(=O)NCc1ccc(Cn2cncn2)cc1`
ZINC58481768 ZINC	0.567	336.4 Da LogP 2.41 TPSA 69.0	✓ Ro5	✓ Clean	`C[C@@H](Oc1ccccc1)C(=O)NCc1ccc(Cn2cncn2)cc1`
ZINC32904430 ZINC	0.561	312.4 Da LogP 2.25 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(Cc1cccs1)NCc1ccc(Cn2cncn2)cc1`
ZINC32818630 ZINC	0.544	322.4 Da LogP 2.02 TPSA 69.0	✓ Ro5	✓ Clean	`O=C(COc1ccccc1)NCc1ccccc1Cn1cncn1`
ZINC585150491 ZINC	0.525	290.3 Da LogP 0.49 TPSA 78.3	✓ Ro5	✓ Clean	`O=C(COc1ccccc1)NCCOCCn1cncn1`
ZINC767103616 ZINC	0.525	288.4 Da LogP 0.78 TPSA 80.0	✓ Ro5	✓ Clean	`O=C(CCCn1cncn1)N[C@@H](CO)Cc1ccccc1`
ZINC23950802 ZINC	0.525	336.4 Da LogP 2.91 TPSA 69.0	✓ Ro5	✓ Clean	`C[C@@H](Oc1ccccc1)C(=O)N[C@H](C)c1ccc(-n2cncn2)…`
ZINC23950804 ZINC	0.525	336.4 Da LogP 2.91 TPSA 69.0	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@@H](C)Oc1ccccc1)c1ccc(-n2cncn2)…`
ZINC23950806 ZINC	0.525	336.4 Da LogP 2.91 TPSA 69.0	✓ Ro5	✓ Clean	`C[C@H](Oc1ccccc1)C(=O)N[C@H](C)c1ccc(-n2cncn2)c…`
ZINC23950808 ZINC	0.525	336.4 Da LogP 2.91 TPSA 69.0	✓ Ro5	✓ Clean	`C[C@H](Oc1ccccc1)C(=O)N[C@@H](C)c1ccc(-n2cncn2)…`
ZINC55968721 ZINC	0.517	324.4 Da LogP 3.06 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(CSc1ccccc1)Nc1ccccc1Cn1cncn1`
ZINC55968998 ZINC	0.517	306.4 Da LogP 2.90 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(CCc1ccccc1)Nc1ccccc1Cn1cncn1`
ZINC71185604 ZINC	0.517	264.4 Da LogP 1.48 TPSA 59.8	✓ Ro5	✓ Clean	`C[C@@H](Cc1cccs1)NC(=O)CCn1cncn1`
ZINC71185605 ZINC	0.517	264.4 Da LogP 1.48 TPSA 59.8	✓ Ro5	✓ Clean	`C[C@H](Cc1cccs1)NC(=O)CCn1cncn1`
ZINC23404910 ZINC	0.509	236.3 Da LogP 1.05 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(CCn1cncn1)NCc1cccs1`
ZINC12974659 ZINC	0.508	322.4 Da LogP 2.52 TPSA 69.0	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)COc1ccccc1)c1ccc(-n2cncn2)cc1`
ZINC12974661 ZINC	0.508	322.4 Da LogP 2.52 TPSA 69.0	✓ Ro5	✓ Clean	`C[C@H](NC(=O)COc1ccccc1)c1ccc(-n2cncn2)cc1`
ZINC25691862 ZINC	0.508	312.4 Da LogP 2.75 TPSA 59.8	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)Cc1cccs1)c1ccc(-n2cncn2)cc1`
ZINC25691866 ZINC	0.508	312.4 Da LogP 2.75 TPSA 59.8	✓ Ro5	✓ Clean	`C[C@H](NC(=O)Cc1cccs1)c1ccc(-n2cncn2)cc1`
ZINC43246290 ZINC	0.508	338.4 Da LogP 2.37 TPSA 78.3	✓ Ro5	✓ Clean	`O=C(COc1ccccc1)Nc1cccc(OCCn2cncn2)c1`
ZINC952964804 ZINC	0.508	286.3 Da LogP 1.20 TPSA 60.2	✓ Ro5	✓ Clean	`C[C@@H](Oc1ccccc1)C(=O)N1CC(Cn2cncn2)C1`
ZINC952964814 ZINC	0.508	286.3 Da LogP 1.20 TPSA 60.2	✓ Ro5	✓ Clean	`C[C@H](Oc1ccccc1)C(=O)N1CC(Cn2cncn2)C1`
ZINC222782383 ZINC	0.500	335.4 Da LogP 2.55 TPSA 72.7	✓ Ro5	✓ Clean	`O=C(CCc1cccnc1)N[C@@H](CCn1cncn1)c1ccccc1`
ZINC222782450 ZINC	0.500	335.4 Da LogP 2.55 TPSA 72.7	✓ Ro5	✓ Clean	`O=C(CCc1cccnc1)N[C@H](CCn1cncn1)c1ccccc1`
ZINC23735477 ZINC	0.500	244.3 Da LogP 1.03 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(CCn1cncn1)NCCc1ccccc1`
ZINC31778 ZINC	0.500	235.3 Da LogP 2.76 TPSA 38.3	✓ Ro5	✓ Clean	`CCC(CC)NC(=O)[C@@H](C)Oc1ccccc1`
ZINC42501941 ZINC	0.500	249.3 Da LogP 1.69 TPSA 46.9	✓ Ro5	✓ Clean	`C[C@@H](Cn1cccn1)NC(=O)Cc1cccs1`
ZINC42501944 ZINC	0.500	249.3 Da LogP 1.69 TPSA 46.9	✓ Ro5	✓ Clean	`C[C@H](Cn1cccn1)NC(=O)Cc1cccs1`
ZINC4675339 ZINC	0.500	235.3 Da LogP 2.76 TPSA 38.3	✓ Ro5	✓ Clean	`CCC(CC)NC(=O)[C@H](C)Oc1ccccc1`
ZINC67872208 ZINC	0.500	263.4 Da LogP 2.08 TPSA 46.9	✓ Ro5	✓ Clean	`CC[C@@H](Cn1ccnc1)NC(=O)Cc1cccs1`
ZINC67872210 ZINC	0.500	263.4 Da LogP 2.08 TPSA 46.9	✓ Ro5	✓ Clean	`CC[C@H](Cn1ccnc1)NC(=O)Cc1cccs1`

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 A0A0H3GV71

Chemistry

ChEMBL CHEMBL50542 ChEMBL CHEMBL63035 ChEMBL CHEMBL60155 ChEMBL CHEMBL303762 ChEMBL CHEMBL418642 ChEMBL CHEMBL62933 ChEMBL CHEMBL423851 ChEMBL CHEMBL64769 ChEMBL CHEMBL66416 ChEMBL CHEMBL304038 ChEMBL CHEMBL63147 ChEMBL CHEMBL65577 ChEMBL CHEMBL293612 ChEMBL CHEMBL294077 ChEMBL CHEMBL294774