Protein profile

KP13_03018

Imidazolonepropionase

Genome: KpKP13

Gene: hutI AHE45598.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GQF7

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Amino acids 439

Annotations 10

Features 18

PDB binders 4

Druggability 0.465

Overview

Basic information about this protein and its source genome.

Accession: KP13_03018
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: hutI AHE45598.1
Status: annotated
Amino acids: 439
Structure source: AlphaFold + ColabFold

3.5.2.7

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+.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 34.085
Human E-value: 1.4399999999999994e-54
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 91.37

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.465

Structure A0A0H3GQF7

Pocket Pocket 14

P2Rank 0.878

Structure A0A0H3GQF7

Pocket Pocket 1

ColabFold model

FPocket 0.471 · Pocket 13

P2Rank 0.884 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 125 / 4744 genomes with a hit

Normalized 0.026

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

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 Features

Domain/signature hits 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; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GQF7	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_03018	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
14				0.465

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	19.19	0.836
2	2.08	0.047
3	0.75	0.002

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
13				0.471

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				19.43	0.839
2				0.84	0.003

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

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	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	2G3F	P42084	126.1 Da LogP -0.06 TPSA 62.0	✓ Ro5	✓ Clean	`C1N=CC(=N1)CC(=O)O`
NCD	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	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	Q81WF0	—	296.4 Da LogP 1.71 TPSA 57.7	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCCC2)cc1`
CHEMBL4580389	Q81WF0	—	150.2 Da LogP 1.54 TPSA 17.0	✓ Ro5	✓ Clean	`CCC1NCCn2cccc21`
CHEMBL4580574	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	1.000	296.4 Da LogP 1.71 TPSA 57.7	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCCC2)cc1`
ZINC16577096	0.971	324.4 Da LogP 2.49 TPSA 57.7	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCCCCC2)cc1`
ZINC6729875	0.971	310.4 Da LogP 2.10 TPSA 57.7	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCCCC2)cc1`
ZINC6730034	0.775	312.4 Da LogP 0.94 TPSA 66.9	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)N2CCOCC2)cc1`
ZINC13669406	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	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	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	0.737	282.4 Da LogP 1.32 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCC2)cc1)S(C)(=O)=O`
ZINC67612464	0.725	310.4 Da LogP 2.10 TPSA 57.7	✓ Ro5	✓ Clean	`CCN(c1ccc(C(=O)N2CCCC2)cc1)S(=O)(=O)CC`
ZINC20245479	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	0.718	296.4 Da LogP 1.71 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCCC2)cc1)S(C)(=O)=O`
ZINC382663	0.718	310.4 Da LogP 2.10 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCCCC2)cc1)S(C)(=O)=O`
ZINC65362493	0.707	324.4 Da LogP 2.49 TPSA 57.7	✓ Ro5	✓ Clean	`CCN(c1ccc(C(=O)N2CCCCC2)cc1)S(=O)(=O)CC`
ZINC65363252	0.707	338.5 Da LogP 2.88 TPSA 57.7	✓ Ro5	✓ Clean	`CCN(c1ccc(C(=O)N2CCCCCC2)cc1)S(=O)(=O)CC`
ZINC16579324	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	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	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	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	0.667	212.3 Da LogP 2.38 TPSA 17.0	✓ Ro5	✓ Clean	`c1ccc(C[C@@H]2NCCn3cccc32)cc1`
ZINC186720	0.667	212.3 Da LogP 2.38 TPSA 17.0	✓ Ro5	✓ Clean	`c1ccc(C[C@H]2NCCn3cccc32)cc1`
ZINC3208092	0.655	200.2 Da LogP -1.17 TPSA 112.6	✓ Ro5	✓ Clean	`O=C(O)CCC1C(=O)NC(=O)NC1=O`
ZINC14000184	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	0.651	344.4 Da LogP 2.75 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCC2)cc1)S(=O)(=O)c1ccccc1`
ZINC284878	0.649	218.3 Da LogP 1.99 TPSA 23.6	✓ Ro5	✓ Clean	`CN(C)c1ccc(C(=O)N2CCCC2)cc1`
ZINC6697643	0.649	243.3 Da LogP 1.17 TPSA 74.7	✓ Ro5	✓ Clean	`CCS(=O)(=O)N(C)c1ccc(C(=O)O)cc1`
ZINC17070361	0.643	296.4 Da LogP 1.71 TPSA 57.7	✓ Ro5	✓ Clean	`CCN(c1ccc(C(=O)N2CCCC2)cc1)S(C)(=O)=O`
ZINC16578683	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	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	0.636	372.5 Da LogP 3.53 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCCCC2)cc1)S(=O)(=O)c1ccccc1`
ZINC835437	0.636	358.5 Da LogP 3.14 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCCC2)cc1)S(=O)(=O)c1ccccc1`
ZINC16577154	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	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	0.632	246.4 Da LogP 2.77 TPSA 23.6	✓ Ro5	✓ Clean	`CN(C)c1ccc(C(=O)N2CCCCCC2)cc1`
ZINC288043	0.632	232.3 Da LogP 2.38 TPSA 23.6	✓ Ro5	✓ Clean	`CN(C)c1ccc(C(=O)N2CCCCC2)cc1`
ZINC3683717	0.632	230.3 Da LogP 2.51 TPSA 17.0	✓ Ro5	✓ Clean	`Fc1ccc(C[C@@H]2NCCn3cccc32)cc1`
ZINC3683718	0.632	230.3 Da LogP 2.51 TPSA 17.0	✓ Ro5	✓ Clean	`Fc1ccc(C[C@H]2NCCn3cccc32)cc1`
ZINC57970741	0.632	260.4 Da LogP 3.16 TPSA 23.6	✓ Ro5	✓ Clean	`CN(C)c1ccc(C(=O)N2CCCCCCC2)cc1`
ZINC16625788	0.628	324.4 Da LogP 2.49 TPSA 57.7	✓ Ro5	✓ Clean	`CCN(c1ccc(C(=O)N2CCCCCC2)cc1)S(C)(=O)=O`
ZINC16626108	0.628	310.4 Da LogP 2.10 TPSA 57.7	✓ Ro5	✓ Clean	`CCN(c1ccc(C(=O)N2CCCCC2)cc1)S(C)(=O)=O`
ZINC226543	0.625	260.4 Da LogP 3.16 TPSA 23.6	✓ Ro5	✓ Clean	`CCN(CC)c1ccc(C(=O)N2CCCCC2)cc1`
ZINC1116635	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	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	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	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	0.615	226.3 Da LogP 2.77 TPSA 17.0	✓ Ro5	✓ Clean	`c1ccc(CC[C@@H]2NCCn3cccc32)cc1`
ZINC771851	0.615	226.3 Da LogP 2.77 TPSA 17.0	✓ Ro5	✓ Clean	`c1ccc(CC[C@H]2NCCn3cccc32)cc1`
ZINC3343824	0.614	344.4 Da LogP 2.75 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccccc1)S(=O)(=O)c1ccc(C(=O)N2CCCC2)cc1`
ZINC4498234	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	0.609	350.5 Da LogP 2.81 TPSA 57.7	✓ Ro5	✓ Clean	`CN(c1ccc(C(=O)N2CCCC2)cc1)S(=O)(=O)c1cccs1`
ZINC2876798	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.