KpATCC43816 Protein target profile

imidazolonepropionase

Accession: VK055_1739

Gene: AIK80359.1 hutI 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GQF7

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Length 405

Pocket druggability (P2Rank · AlphaFold DB model) 0.878

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 53 total records

Functional annotation 1 EC 9 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Metabolic chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Central metabolic position More central than 89.7% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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 (%): 33.753 Lower values reduce human off-target concern.
Human E-value: 1.3499999999999998e-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 (%): 38.542 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 96.27 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 0.916 · Pocket 1

FPocket 0.707 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 125 / 4744 genomes with a hit

Prevalence 2.6%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Attractive metabolic target: catalyzes a producing chokepoint reaction in Histidine metabolism, no isoenzyme backup detected, more central than 89.7% of genes in this genome.

Relative network centrality 89.7% more central than 89.7% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MTEATSELVIWRNGRLATLNPDHAQPYGLLERHALLVRDGRIVAIVAEDDVPSGRSIDLEGRLVTPGLIDCHTHLVFGGSRAQEWEQRLNGVSYQTISASGGGINSTVRATRDSSEAELLALAQPRLERLLREGVTTLEIKSGYGLDLPNERKMLRVARQLADHNGVELSATLLSAHATPPEYQGDANGYITLVCETILPTLWQEGLFESVDVFCENVGFSPQQTERVFQAAQALGIPVKGHVEQLSSLGGAQLVSRYHGLSADHIEYLTEEGVAAMRESGTVAALLPGAFYFLNETRKPPVELLRKYQVPMAVATDFNPGTSPFASLHLAMNMACVKFGLTPEEAWAGVTRHAARALGRQASHGQLAPGFVANFAIWDAEHPVEMVYEPGRSPLWHRVVQGELQ

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: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:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0016812 Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a cyclic amide.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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
67	365	FunFam	G3DSA:3.20.20.140:FF:000007	Imidazolonepropionase
66	365	SUPERFAMILY	SSF51556	Metallo-dependent hydrolases
66	365	InterPro	IPR032466	Metal-dependent hydrolase
35	391	CDD	cd01296	Imidazolone-5PH
35	391	InterPro	IPR005920	Imidazolonepropionase
14	402	Gene3D	G3DSA:2.30.40.10	Urease, subunit C, domain 1
14	402	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
5	403	PANTHER	PTHR42752	IMIDAZOLONEPROPIONASE
5	403	InterPro	IPR005920	Imidazolonepropionase
7	405	Hamap	MF_00372	Imidazolonepropionase [hutI].
7	405	InterPro	IPR005920	Imidazolonepropionase
9	404	SUPERFAMILY	SSF51338	Composite domain of metallo-dependent hydrolases
9	404	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
63	383	Pfam	PF01979	Amidohydrolase family
63	383	InterPro	IPR006680	Amidohydrolase-related
31	403	NCBIfam	TIGR01224	imidazolonepropionase
31	403	InterPro	IPR005920	Imidazolonepropionase
67	365	Gene3D	G3DSA:3.20.20.140	-

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

Show in viewer

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

0.916

Likely same site as FPocket 1 0.6 Å 20 shared residues 95% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.082

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Surrounding area

Pocket 3 P2Rank #3

0.006

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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

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

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 VK055_1739	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.

53 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 0 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

NIG PDB via homolog Detail RCSB PDB

ZINC116840878 ZINC proposed compound · Tanimoto 0.704 Detail ZINC

ZINC2560884 ZINC proposed compound · Tanimoto 0.704 Detail ZINC

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`
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).

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
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`
ZINC3208092 ZINC	0.655	200.2 Da LogP -1.17 TPSA 112.6	✓ Ro5	✓ Clean	`O=C(O)CCC1C(=O)NC(=O)NC1=O`
ZINC22215812 ZINC	0.600	220.2 Da LogP 1.28 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)CC[C@@H]1Nc2ccccc2NC1=O`
ZINC22215815 ZINC	0.600	220.2 Da LogP 1.28 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)CC[C@H]1Nc2ccccc2NC1=O`
ZINC8076668 ZINC	0.576	200.2 Da LogP -1.15 TPSA 95.5	✓ Ro5	✓ Clean	`C[C@@H]1NC(=O)[C@H](CCC(=O)O)NC1=O`
ZINC1116258333 ZINC	0.568	253.3 Da LogP 0.37 TPSA 78.5	✓ Ro5	✓ Clean	`C[C@H]1CC[C@@H](C)N1C(=O)CC[C@@H]1NC(=O)NC1=O`
ZINC32843863 ZINC	0.568	267.3 Da LogP 0.77 TPSA 78.5	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](CCC(=O)N2CCCCCCC2)N1`
ZINC32843864 ZINC	0.568	267.3 Da LogP 0.77 TPSA 78.5	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](CCC(=O)N2CCCCCCC2)N1`
ZINC46463395 ZINC	0.568	253.3 Da LogP 0.38 TPSA 78.5	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](CCC(=O)N2CCCCCC2)N1`
ZINC14141965 ZINC	0.553	267.3 Da LogP 0.81 TPSA 87.3	✓ Ro5	✓ Clean	`O=C(CC[C@@H]1NC(=O)NC1=O)NC1CCCCCC1`
ZINC14141966 ZINC	0.553	267.3 Da LogP 0.81 TPSA 87.3	✓ Ro5	✓ Clean	`O=C(CC[C@H]1NC(=O)NC1=O)NC1CCCCCC1`
ZINC952984289 ZINC	0.553	257.3 Da LogP -0.06 TPSA 78.5	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](CCC(=O)N2CCC(F)CC2)N1`
ZINC220160890 ZINC	0.543	242.3 Da LogP -0.12 TPSA 95.5	✓ Ro5	✓ Clean	`CC(C)C[C@H]1NC(=O)[C@@H](CCC(=O)O)NC1=O`
ZINC220160960 ZINC	0.543	242.3 Da LogP -0.12 TPSA 95.5	✓ Ro5	✓ Clean	`CC(C)C[C@@H]1NC(=O)[C@@H](CCC(=O)O)NC1=O`
ZINC220161024 ZINC	0.543	242.3 Da LogP -0.12 TPSA 95.5	✓ Ro5	✓ Clean	`CC(C)C[C@H]1NC(=O)[C@H](CCC(=O)O)NC1=O`
ZINC35079158 ZINC	0.543	242.3 Da LogP -0.12 TPSA 95.5	✓ Ro5	✓ Clean	`CC(C)C[C@@H]1NC(=O)[C@H](CCC(=O)O)NC1=O`
ZINC2161326 ZINC	0.538	248.2 Da LogP 0.60 TPSA 95.5	✓ Ro5	✓ Clean	`O=C(O)CC[C@@H]1NC(=O)c2ccccc2NC1=O`
ZINC49215456 ZINC	0.538	257.3 Da LogP -0.45 TPSA 78.5	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](CCC(=O)N2CCSCC2)N1`
ZINC580072 ZINC	0.538	248.2 Da LogP 0.60 TPSA 95.5	✓ Ro5	✓ Clean	`O=C(O)CC[C@H]1NC(=O)c2ccccc2NC1=O`
ZINC585079693 ZINC	0.538	281.4 Da LogP 0.77 TPSA 87.3	✓ Ro5	✓ Clean	`CC1(C)C(CNC(=O)CC[C@H]2NC(=O)NC2=O)C1(C)C`
ZINC585079694 ZINC	0.538	281.4 Da LogP 0.77 TPSA 87.3	✓ Ro5	✓ Clean	`CC1(C)C(CNC(=O)CC[C@@H]2NC(=O)NC2=O)C1(C)C`
ZINC642014463 ZINC	0.537	337.4 Da LogP 1.88 TPSA 87.3	✓ Ro5	✓ Clean	`O=C(CC[C@@H]1NC(=O)NC1=O)NC(c1ccccc1)c1ccccc1`
ZINC33023504 ZINC	0.525	281.7 Da LogP 1.27 TPSA 87.3	✓ Ro5	✓ Clean	`O=C(CC[C@@H]1NC(=O)NC1=O)Nc1ccc(Cl)cc1`
ZINC33023506 ZINC	0.525	281.7 Da LogP 1.27 TPSA 87.3	✓ Ro5	✓ Clean	`O=C(CC[C@H]1NC(=O)NC1=O)Nc1ccc(Cl)cc1`
ZINC33023984 ZINC	0.525	265.2 Da LogP 0.75 TPSA 87.3	✓ Ro5	✓ Clean	`O=C(CC[C@@H]1NC(=O)NC1=O)Nc1ccc(F)cc1`
ZINC33023987 ZINC	0.525	265.2 Da LogP 0.75 TPSA 87.3	✓ Ro5	✓ Clean	`O=C(CC[C@H]1NC(=O)NC1=O)Nc1ccc(F)cc1`
ZINC952962109 ZINC	0.525	267.2 Da LogP -0.00 TPSA 78.5	✓ Ro5	✓ Clean	`CN(CC(F)(F)F)C(=O)CC[C@@H]1NC(=O)NC1=O`
ZINC952983648 ZINC	0.525	239.3 Da LogP 0.03 TPSA 87.3	✓ Ro5	✓ Clean	`CC1(NC(=O)CC[C@@H]2NC(=O)NC2=O)CCC1`
ZINC31971003 ZINC	0.524	275.3 Da LogP 0.33 TPSA 87.3	✓ Ro5	✓ Clean	`O=C(CC[C@@H]1NC(=O)NC1=O)NCCc1ccccc1`
ZINC31971004 ZINC	0.524	275.3 Da LogP 0.33 TPSA 87.3	✓ Ro5	✓ Clean	`O=C(CC[C@H]1NC(=O)NC1=O)NCCc1ccccc1`
ZINC375284974 ZINC	0.524	309.4 Da LogP 0.39 TPSA 87.7	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](CCC(=O)N2CCC3(CCOCC3)CC2)N1`
ZINC817863294 ZINC	0.524	285.3 Da LogP -0.41 TPSA 124.6	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)CC[C@@H]1NC(=O)NC1=O)C(=O)O`
ZINC3290147 ZINC	0.514	204.2 Da LogP 0.83 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](CCc2ccccc2)N1`
ZINC3290149 ZINC	0.514	204.2 Da LogP 0.83 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](CCc2ccccc2)N1`
ZINC1290648834 ZINC	0.512	257.2 Da LogP -1.39 TPSA 104.8	✓ Ro5	✓ Clean	`COC(=O)CN(C)C(=O)CC[C@@H]1NC(=O)NC1=O`
ZINC1800407951 ZINC	0.512	281.3 Da LogP -0.80 TPSA 98.7	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](CCC(=O)N2C[C@H]3C[C@H](O)C[C@H]…`
ZINC1800410722 ZINC	0.512	281.3 Da LogP -0.80 TPSA 98.7	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](CCC(=O)N2C[C@H]3C[C@@H](O)C[C@H…`
ZINC298211597 ZINC	0.512	269.3 Da LogP -0.39 TPSA 87.7	✓ Ro5	✓ Clean	`C[C@H]1CN(C(=O)CC[C@@H]2NC(=O)NC2=O)C[C@@H](C)O1`
ZINC32845419 ZINC	0.512	281.4 Da LogP 1.01 TPSA 78.5	✓ Ro5	✓ Clean	`CC1CCC(N(C)C(=O)CC[C@@H]2NC(=O)NC2=O)CC1`
ZINC32845420 ZINC	0.512	281.4 Da LogP 1.01 TPSA 78.5	✓ Ro5	✓ Clean	`CC1CCC(N(C)C(=O)CC[C@H]2NC(=O)NC2=O)CC1`
ZINC61532389 ZINC	0.512	257.2 Da LogP -1.39 TPSA 104.8	✓ Ro5	✓ Clean	`COC(=O)CN(C)C(=O)CC[C@H]1NC(=O)NC1=O`
ZINC642111927 ZINC	0.512	281.4 Da LogP 1.16 TPSA 78.5	✓ Ro5	✓ Clean	`CCN(C(=O)CC[C@@H]1NC(=O)NC1=O)C1CCCCC1`
ZINC68193206 ZINC	0.512	326.1 Da LogP 1.38 TPSA 87.3	✓ Ro5	✓ Clean	`O=C(CC[C@H]1NC(=O)NC1=O)Nc1ccc(Br)cc1`
ZINC68193207 ZINC	0.512	326.1 Da LogP 1.38 TPSA 87.3	✓ Ro5	✓ Clean	`O=C(CC[C@@H]1NC(=O)NC1=O)Nc1ccc(Br)cc1`
ZINC952982722 ZINC	0.512	277.3 Da LogP 0.40 TPSA 78.5	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](CCC(=O)N2C[C@H]3CC=CC[C@H]3C2)N1`
ZINC819142317 ZINC	0.512	305.3 Da LogP -0.08 TPSA 124.6	✓ Ro5	✓ Clean	`O=C(CC[C@@H]1NC(=O)NC1=O)N[C@H](C(=O)O)c1ccccc1`
ZINC12903744 ZINC	0.500	267.3 Da LogP 0.67 TPSA 87.3	✓ Ro5	✓ Clean	`C[C@@H]1CCCC[C@@H]1NC(=O)CC[C@@H]1NC(=O)NC1=O`
ZINC13097148 ZINC	0.500	316.4 Da LogP 0.32 TPSA 81.8	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](CCC(=O)N2CCN(c3ccccc3)CC2)N1`

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

Pathways

KEGG R02288 BioCyc IMIDAZOLONEPROPIONASE-RXN