KpKP13 Protein target profile

Imidazolonepropionase

Accession: KP13_03018

Gene: AHE45598.1 hutI 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GQF7

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Length 439

Pocket druggability (P2Rank · AlphaFold DB model) 0.878

Direct ligand evidence 0 57 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 0.47. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.88. 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 (%): 34.085 Lower values reduce human off-target concern.
Human E-value: 1.4399999999999994e-54
Gut microbiome similarity: 2.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 91.37 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) 0.878

Structure A0A0H3GQF7

Pocket Pocket 1

Druggability (FPocket) 0.465

Structure A0A0H3GQF7

Pocket Pocket 14

ColabFold model

P2Rank 0.884 · Pocket 1

FPocket 0.471 · Pocket 13

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 125 / 4744 genomes with a hit

Prevalence 2.6%

Sequence

Primary amino-acid sequence viewer.

MVFSHKKITFPCAIVDFTGVMKINVYTTHDKLSAMTEATSELVIWRNGRLATLNPDHAQPYGLLERHALLVRDGRIAAIVAEDDVPSGRSIDLEGRLVTPGLIDCHTHLVFGGSRAQEWEQRLNGVSYQTISASGGGINSTVRATRDSSEAELLALAQPRLERLLREGVTTLEIKSGYGLDLPNERKMLRVARQLADHNGVELSATLLSAHATPPEYQGDADGYITLVCETILPTLWQEGLFESVDVFCENVGFSPQQTERVFQAAQALGIPVKGHVEQLSSLGGAQLVSRYHGLSADHIEYLTEEGVAAMRESGTVAALLPGAFYFLNETRKPPVELLRKYQVPMAVATDFNPGTSPFASLHLAMNMACVKFGLTPEEAWAGVTRHAARALGRQASHGQLAPGFVANFAIWDAEHPVEMVYEPGRSPLWHRVVQGELQ

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

3.5.2.7

Gene Ontology (GO)

GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0016810 Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds.
GO:0019556 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-histidine into other compounds, including glutamate and formamide.
GO:0016812 Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a cyclic amide.
GO:0050480 Catalysis of the reaction: (S)-3-(4-oxo-4,5-dihydro-1H-imidazol-5-yl)propanoic acid + H2O = N-formimidoyl-L-glutamate + H+.
GO:0005506 Binding to an iron (Fe) ion.
GO:0008270 Binding to a zinc ion (Zn).
GO:0019557 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-histidine into other compounds, including glutamate and formate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

18 records

Show feature table

Start	End	DB	Term	Name
65	437	NCBIfam	TIGR01224	imidazolonepropionase
65	437	InterPro	IPR005920	Imidazolonepropionase
43	438	SUPERFAMILY	SSF51338	Composite domain of metallo-dependent hydrolases
43	438	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
97	417	Pfam	PF01979	Amidohydrolase family
97	417	InterPro	IPR006680	Amidohydrolase-related
101	399	FunFam	G3DSA:3.20.20.140:FF:000007	Imidazolonepropionase
100	399	SUPERFAMILY	SSF51556	Metallo-dependent hydrolases
100	399	InterPro	IPR032466	Metal-dependent hydrolase
48	436	Gene3D	G3DSA:2.30.40.10	Urease, subunit C, domain 1
48	436	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
69	425	CDD	cd01296	Imidazolone-5PH
69	425	InterPro	IPR005920	Imidazolonepropionase
101	399	Gene3D	G3DSA:3.20.20.140	-
41	439	Hamap	MF_00372	Imidazolonepropionase [hutI].
41	439	InterPro	IPR005920	Imidazolonepropionase
35	437	PANTHER	PTHR42752	IMIDAZOLONEPROPIONASE
35	437	InterPro	IPR005920	Imidazolonepropionase

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

0.878

Likely same site as FPocket 14 1.3 Å 20 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.107

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Surrounding area

Pocket 3 P2Rank #3

0.028

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Surrounding area

Pocket 4 P2Rank #4

0.005

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Surrounding area

Pocket 5 P2Rank #5

0.005

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #14

0.465

Likely same site as P2Rank 1 1.3 Å 20 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Binding site:106-106

UniProt: Binding site:108-108

UniProt: Binding site:115-115

UniProt: Binding site:178-178

UniProt: Binding site:211-211

UniProt: Binding site:276-276

UniProt: Binding site:279-279

UniProt: Binding site:351-351

UniProt: Binding site:353-353

UniProt: Binding site:355-355

UniProt: Binding site:356-356

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.884

Likely same site as FPocket 13 1.0 Å 19 shared residues 95% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.044

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Surrounding area

Pocket 3 P2Rank #3

0.041

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Surrounding area

Pocket 4 P2Rank #4

0.031

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Surrounding area

Pocket 5 P2Rank #5

0.016

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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_A0A0H3GQF7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03018	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.

57 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 3 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

DI6 PDB via homolog 172.1 Da · LogP -0.94 · TPSA 95.5 Open detail RCSB PDB

IZC PDB via homolog Detail RCSB PDB

NCD PDB via homolog Detail RCSB PDB

NIG PDB via homolog Detail RCSB PDB

CHEMBL4532317 ChEMBL via homolog Detail ChEMBL

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
DI6 RCSB PDB	2Q09	A0KF84	172.1 Da LogP -0.94 TPSA 95.5	✓ Ro5	✓ Clean	`C(CC(=O)O)[C@H]1C(=O)NC(=O)N1`
IZC RCSB PDB	2G3F	P42084	126.1 Da LogP -0.06 TPSA 62.0	✓ Ro5	✓ Clean	`C1N=CC(=N1)CC(=O)O`
NCD RCSB PDB	4YIW	Q81WF0	176.1 Da LogP -1.42 TPSA 129.7	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)NC(=O)N)C(=O)O`
NIG RCSB PDB	2PUZ	Q8U8Z6	174.2 Da LogP -0.50 TPSA 110.5	✓ Ro5	✓ Clean	`[H]/N=C\N[C@@H](CCC(=O)O)C(=O)O`

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
CHEMBL4532317 ChEMBL	Q81WF0	—	296.4 Da LogP 1.71 TPSA 57.7	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCCC2)cc1`
CHEMBL4580389 ChEMBL	Q81WF0	—	150.2 Da LogP 1.54 TPSA 17.0	✓ Ro5	✓ Clean	`CCC1NCCn2cccc21`
CHEMBL4580574 ChEMBL	Q81WF0	—	161.2 Da LogP 1.67 TPSA 25.2	✓ Ro5	✓ Clean	`Cn1ccc2c(CO)cccc21`

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
ZINC6697094 ZINC	1.000	296.4 Da LogP 1.71 TPSA 57.7	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCCC2)cc1`
ZINC16577096 ZINC	0.971	324.4 Da LogP 2.49 TPSA 57.7	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCCCCC2)cc1`
ZINC6729875 ZINC	0.971	310.4 Da LogP 2.10 TPSA 57.7	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCCCC2)cc1`
ZINC6730034 ZINC	0.775	312.4 Da LogP 0.94 TPSA 66.9	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCOCC2)cc1`
ZINC13669406 ZINC	0.744	324.4 Da LogP 2.34 TPSA 57.7	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCC[C@@H](C)C2)cc1`
ZINC13669407 ZINC	0.744	324.4 Da LogP 2.34 TPSA 57.7	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCC[C@H](C)C2)cc1`
ZINC16577231 ZINC	0.738	383.5 Da LogP 1.39 TPSA 87.2	✓ Ro5	✓ Clean	`CCOC(=O)N1CCN(C(=O)c2ccc(N(C)S(=O)(=O)CC)cc2)CC1`
ZINC800437 ZINC	0.737	282.4 Da LogP 1.32 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCC2)cc1)S(C)(=O)=O`
ZINC67612464 ZINC	0.725	310.4 Da LogP 2.10 TPSA 57.7	✓ Ro5	✓ Clean	`CCN(c1ccc(C(=O)N2CCCC2)cc1)S(=O)(=O)CC`
ZINC20245479 ZINC	0.718	311.4 Da LogP 1.17 TPSA 60.9	✓ Ro5	✓ Clean	`CN(C)S(=O)(=O)N(C)c1ccc(C(=O)N2CCCC2)cc1`
ZINC382492 ZINC	0.718	296.4 Da LogP 1.71 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCCC2)cc1)S(C)(=O)=O`
ZINC382663 ZINC	0.718	310.4 Da LogP 2.10 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCCCC2)cc1)S(C)(=O)=O`
ZINC65362493 ZINC	0.707	324.4 Da LogP 2.49 TPSA 57.7	✓ Ro5	✓ Clean	`CCN(c1ccc(C(=O)N2CCCCC2)cc1)S(=O)(=O)CC`
ZINC65363252 ZINC	0.707	338.5 Da LogP 2.88 TPSA 57.7	✓ Ro5	✓ Clean	`CCN(c1ccc(C(=O)N2CCCCCC2)cc1)S(=O)(=O)CC`
ZINC16579324 ZINC	0.705	387.5 Da LogP 2.43 TPSA 60.9	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCN(c3ccccc3)CC2)cc1`
ZINC116840878 ZINC	0.704	258.2 Da LogP -1.30 TPSA 132.8	✓ Ro5	✓ Clean	`O=C(O)CC[C@@H]1NC(=O)[C@@H](CCC(=O)O)NC1=O`
ZINC2560884 ZINC	0.704	258.2 Da LogP -1.30 TPSA 132.8	✓ Ro5	✓ Clean	`O=C(O)CC[C@H]1NC(=O)[C@@H](CCC(=O)O)NC1=O`
ZINC4899712 ZINC	0.704	258.2 Da LogP -1.30 TPSA 132.8	✓ Ro5	✓ Clean	`O=C(O)CC[C@@H]1NC(=O)[C@H](CCC(=O)O)NC1=O`
ZINC186715 ZINC	0.667	212.3 Da LogP 2.38 TPSA 17.0	✓ Ro5	✓ Clean	`c1ccc(C[C@@H]2NCCn3cccc32)cc1`
ZINC186720 ZINC	0.667	212.3 Da LogP 2.38 TPSA 17.0	✓ Ro5	✓ Clean	`c1ccc(C[C@H]2NCCn3cccc32)cc1`
ZINC3208092 ZINC	0.655	200.2 Da LogP -1.17 TPSA 112.6	✓ Ro5	✓ Clean	`O=C(O)CCC1C(=O)NC(=O)NC1=O`
ZINC14000184 ZINC	0.653	415.5 Da LogP 2.96 TPSA 86.8	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)Nc2ccccc2C(=O)N2CCCC2…`
ZINC269512 ZINC	0.651	344.4 Da LogP 2.75 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCC2)cc1)S(=O)(=O)c1ccccc1`
ZINC284878 ZINC	0.649	218.3 Da LogP 1.99 TPSA 23.6	✓ Ro5	✓ Clean	`CN(C)c1ccc(C(=O)N2CCCC2)cc1`
ZINC6697643 ZINC	0.649	243.3 Da LogP 1.17 TPSA 74.7	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)O)cc1`
ZINC17070361 ZINC	0.643	296.4 Da LogP 1.71 TPSA 57.7	✓ Ro5	✓ Clean	`CCN(c1ccc(C(=O)N2CCCC2)cc1)S(C)(=O)=O`
ZINC16578683 ZINC	0.640	429.5 Da LogP 3.35 TPSA 86.8	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)Nc2ccccc2C(=O)N2CCCCC…`
ZINC1144954 ZINC	0.636	358.5 Da LogP 3.06 TPSA 57.7	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)N(C)c2ccc(C(=O)N3CCCC3)cc2)cc1`
ZINC3331522 ZINC	0.636	372.5 Da LogP 3.53 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCCCC2)cc1)S(=O)(=O)c1ccccc1`
ZINC835437 ZINC	0.636	358.5 Da LogP 3.14 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCCC2)cc1)S(=O)(=O)c1ccccc1`
ZINC16577154 ZINC	0.633	422.0 Da LogP 3.09 TPSA 60.9	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCN(c3cccc(Cl)c3)CC…`
ZINC16578820 ZINC	0.633	415.6 Da LogP 3.05 TPSA 60.9	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCN(c3cccc(C)c3C)CC…`
ZINC284866 ZINC	0.632	246.4 Da LogP 2.77 TPSA 23.6	✓ Ro5	✓ Clean	`CN(C)c1ccc(C(=O)N2CCCCCC2)cc1`
ZINC288043 ZINC	0.632	232.3 Da LogP 2.38 TPSA 23.6	✓ Ro5	✓ Clean	`CN(C)c1ccc(C(=O)N2CCCCC2)cc1`
ZINC3683717 ZINC	0.632	230.3 Da LogP 2.51 TPSA 17.0	✓ Ro5	✓ Clean	`Fc1ccc(C[C@@H]2NCCn3cccc32)cc1`
ZINC3683718 ZINC	0.632	230.3 Da LogP 2.51 TPSA 17.0	✓ Ro5	✓ Clean	`Fc1ccc(C[C@H]2NCCn3cccc32)cc1`
ZINC57970741 ZINC	0.632	260.4 Da LogP 3.16 TPSA 23.6	✓ Ro5	✓ Clean	`CN(C)c1ccc(C(=O)N2CCCCCCC2)cc1`
ZINC16625788 ZINC	0.628	324.4 Da LogP 2.49 TPSA 57.7	✓ Ro5	✓ Clean	`CCN(c1ccc(C(=O)N2CCCCCC2)cc1)S(C)(=O)=O`
ZINC16626108 ZINC	0.628	310.4 Da LogP 2.10 TPSA 57.7	✓ Ro5	✓ Clean	`CCN(c1ccc(C(=O)N2CCCCC2)cc1)S(C)(=O)=O`
ZINC226543 ZINC	0.625	260.4 Da LogP 3.16 TPSA 23.6	✓ Ro5	✓ Clean	`CCN(CC)c1ccc(C(=O)N2CCCCC2)cc1`
ZINC1116635 ZINC	0.622	378.9 Da LogP 3.40 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCC2)cc1)S(=O)(=O)c1ccc(Cl)cc1`
ZINC2843587 ZINC	0.622	386.5 Da LogP 3.84 TPSA 57.7	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)N(C)c2ccc(C(=O)N3CCCCCC3)cc2)cc1`
ZINC713150 ZINC	0.622	372.5 Da LogP 3.45 TPSA 57.7	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)N(C)c2ccc(C(=O)N3CCCCC3)cc2)cc1`
ZINC16577615 ZINC	0.620	417.5 Da LogP 2.44 TPSA 70.2	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCN(c3ccccc3OC)CC2)…`
ZINC2464493 ZINC	0.615	226.3 Da LogP 2.77 TPSA 17.0	✓ Ro5	✓ Clean	`c1ccc(CC[C@@H]2NCCn3cccc32)cc1`
ZINC771851 ZINC	0.615	226.3 Da LogP 2.77 TPSA 17.0	✓ Ro5	✓ Clean	`c1ccc(CC[C@H]2NCCn3cccc32)cc1`
ZINC3343824 ZINC	0.614	344.4 Da LogP 2.75 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccccc1)S(=O)(=O)c1ccc(C(=O)N2CCCC2)cc1`
ZINC4498234 ZINC	0.614	325.4 Da LogP 0.86 TPSA 60.9	✓ Ro5	✓ Clean	`CCN1CCN(C(=O)c2ccc(N(C)S(C)(=O)=O)cc2)CC1`
ZINC13494677 ZINC	0.609	350.5 Da LogP 2.81 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCC2)cc1)S(=O)(=O)c1cccs1`
ZINC2876798 ZINC	0.609	406.9 Da LogP 4.18 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCCCC2)cc1)S(=O)(=O)c1ccc(Cl)c…`

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 A0A0H3GQF7

Chemistry

ChEMBL CHEMBL4532317 ChEMBL CHEMBL4580389 ChEMBL CHEMBL4580574