KpATCC43816 Protein target profile

argD

Accession: VK055_3730

Gene: AIK82284.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3H3Z1

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Length 406

Pocket druggability (P2Rank · AlphaFold DB model) 0.58

Direct ligand evidence 0 57 total records

Functional annotation 0 EC 5 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 0.55. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.58. Structure available AlphaFold DB model + ColabFold model 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 (%): 38.571 Lower values reduce human off-target concern.
Human E-value: 1.06e-07
Gut microbiome similarity: 3.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 45.876 Higher values support similarity to known essential genes.
DEG E-value: 2.49e-113 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.98 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) 0.58

Structure A0A0H3H3Z1

Pocket Pocket 1

Druggability (FPocket) 0.552

Structure A0A0H3H3Z1

Pocket Pocket 27

ColabFold model

P2Rank 0.522 · Pocket 1

FPocket 0.903 · Pocket 3

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 156 / 4744 genomes with a hit

Prevalence 3.3%

Metabolic context

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

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MATEQPAITRATFDEVILPIYAPAEFIPVKGKGSRVWDQQGKEYIDFAGGIAVTALGHCHPALVAALHQQGETLWHTSNVFTNEPALRLGRKLVEATFAERVVFMNSGTEANETAFKLARHYAVTRHSPYKTKIIAFHNAFHGRSLFTVSVGGQPKYSDGFGPKPADIVHVPFNDLQAVKAVMDDHTCAVVVEPIQGEGGVTAATPAFLQGLCELCDQHQALLVFDEVQCGMGRTGSLFAYMHYGVTPDILTSAKALGGGFPVSAMLTTHEIASAFHAGSHGSTYGGNPLACAVANAAFDLINTPAVLDGVSAKRELFVKHLQRLDAEFDLFSDIRGMGLLIGAELKPQHKGRARDFLYAAADAGVMVLNAGPDVMRFVPSLIIDEQDITEGMARFTQAVAKVING

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0006525 The chemical reactions and pathways involving arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
GO:0008483 Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.
GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
60	305	Gene3D	G3DSA:3.40.640.10	-
60	305	InterPro	IPR015421	Pyridoxal phosphate-dependent transferase, major domain
30	393	Gene3D	G3DSA:3.90.1150.10	Aspartate Aminotransferase, domain 1
30	393	InterPro	IPR015422	Pyridoxal phosphate-dependent transferase, small domain
173	403	PIRSF	PIRSF000521	Transaminase_4ab_Lys_Orn
173	403	InterPro	IPR005814	Aminotransferase class-III
28	157	PIRSF	PIRSF000521	Transaminase_4ab_Lys_Orn
28	157	InterPro	IPR005814	Aminotransferase class-III
223	260	ProSitePatterns	PS00600	Aminotransferases class-III pyridoxal-phosphate attachment site.
223	260	InterPro	IPR005814	Aminotransferase class-III
26	400	Pfam	PF00202	Aminotransferase class-III
26	400	InterPro	IPR005814	Aminotransferase class-III
20	400	SUPERFAMILY	SSF53383	PLP-dependent transferases
20	400	InterPro	IPR015424	Pyridoxal phosphate-dependent transferase
60	305	FunFam	G3DSA:3.40.640.10:FF:000004	Acetylornithine aminotransferase
16	403	Hamap	MF_01107	Acetylornithine/succinyldiaminopimelate aminotransferase [argD].
16	403	InterPro	IPR004636	Acetylornithine/Succinylornithine transaminase family
21	400	CDD	cd00610	OAT_like
21	400	InterPro	IPR005814	Aminotransferase class-III
14	402	PANTHER	PTHR11986	AMINOTRANSFERASE CLASS III
17	400	NCBIfam	TIGR00707	acetylornithine/succinylornithine family transaminase
17	400	InterPro	IPR004636	Acetylornithine/Succinylornithine transaminase family
8	404	NCBIfam	TIGR03246	acetylornithine/succinylornithine family transaminase
8	404	InterPro	IPR017652	Acetyl/Succinylornithine transaminase family, bacteria

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

0.58

Likely same site as FPocket 27 3.1 Å 11 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.522

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Surrounding area

Pocket 3 P2Rank #3

0.283

Likely same site as FPocket 13 2.7 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.053

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Surrounding area

Pocket 5 P2Rank #5

0.047

Likely same site as FPocket 3 3.4 Å 8 shared residues 100% of smaller site

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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 #27

0.552

Likely same site as P2Rank 1 3.1 Å 11 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #13

0.341

Likely same site as P2Rank 3 2.7 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 3 FPocket #3

0.294 Unusual size

Likely same site as P2Rank 5 3.4 Å 8 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Binding site:108-109

UniProt: Binding site:141-141

UniProt: Binding site:144-144

UniProt: Binding site:226-229

UniProt: Binding site:283-283

UniProt: Binding site:284-284

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.522

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Surrounding area

Pocket 2 P2Rank #2

0.499

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Surrounding area

Pocket 3 P2Rank #3

0.213

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Surrounding area

Pocket 4 P2Rank #4

0.116

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Surrounding area

Pocket 5 P2Rank #5

0.112

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Surrounding area

Residue sets

UniProt: Binding site:108-109

UniProt: Binding site:141-141

UniProt: Binding site:144-144

UniProt: Binding site:226-229

UniProt: Binding site:283-283

UniProt: Binding site:284-284

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_A0A0H3H3Z1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3730	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 6 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

P00 PDB via homolog 363.3 Da · LogP -0.14 · TPSA 184.8 Open detail RCSB PDB

POI PDB via homolog Detail RCSB PDB

PPE PDB via homolog Detail RCSB PDB

PXG PDB via homolog Detail RCSB PDB

SUO 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
P00 RCSB PDB	4JEW	P40732	363.3 Da LogP -0.14 TPSA 184.8	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/OCC[C@@H](C(=O)O)…`
POI RCSB PDB	1WKG	Q5SHH5	405.3 Da LogP 0.16 TPSA 178.3	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNCCC[C@@H](C(=O)O)NC(…`
PPE RCSB PDB	1WKH	Q5SHH5	379.3 Da LogP -0.47 TPSA 187.8	1 viol.	✓ Clean	`Cc1c(c(c(c[nH+]1)COP(=O)(O)O)CN[C@@H](CCC(=O)O)…`
PXG RCSB PDB	4JEV	P40732	368.3 Da LogP 2.02 TPSA 149.2	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNc2cccc(c2)C(=O)O)O`
SUO RCSB PDB	4ADD	P77581	232.2 Da LogP -0.84 TPSA 129.7	✓ Ro5	✓ Clean	`C(C[C@@H](C(=O)O)NC(=O)CCC(=O)O)CN`
TNF RCSB PDB	4JEW	P40732	229.1 Da LogP 1.12 TPSA 149.7	✓ Ro5	✓ Clean	`c1c(cc(c(c1[N+](=O)[O-])O)[N+](=O)[O-])[N+](=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
CHEMBL330129 ChEMBL	P29758	—	127.1 Da LogP -0.19 TPSA 63.3	✓ Ro5	✓ Clean	`C#CC(N)CCC(=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
ZINC1883067 ZINC	1.000	229.1 Da LogP 1.12 TPSA 149.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc([N+](=O)[O-])c(O)c([N+](=O)[O-…`
ZINC2170217 ZINC	0.792	200.1 Da LogP 0.91 TPSA 126.7	✓ Ro5	Alert	`O=[N+]([O-])c1cc(O)c(O)c([N+](=O)[O-])c1`
ZINC68564159 ZINC	0.792	366.2 Da LogP 2.40 TPSA 213.0	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(-c2cc([N+](=O)[O-])cc([N+](=O)…`
ZINC34772749 ZINC	0.769	228.1 Da LogP 0.91 TPSA 143.8	✓ Ro5	✓ Clean	`O=C(O)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC1866114950 ZINC	0.758	260.3 Da LogP -0.06 TPSA 129.7	✓ Ro5	✓ Clean	`NCCCC[C@H](NC(=O)CCCC(=O)O)C(=O)O`
ZINC1555225 ZINC	0.731	218.6 Da LogP 1.86 TPSA 106.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(Cl)c(O)c([N+](=O)[O-])c1`
ZINC1657271 ZINC	0.731	263.0 Da LogP 1.97 TPSA 106.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(Br)c(O)c([N+](=O)[O-])c1`
ZINC34261082 ZINC	0.731	202.1 Da LogP 1.35 TPSA 106.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(F)c(O)c([N+](=O)[O-])c1`
ZINC1530138 ZINC	0.719	217.3 Da LogP -0.97 TPSA 118.4	✓ Ro5	✓ Clean	`NCCCC[C@H](NC(=O)CCN)C(=O)O`
ZINC15261541 ZINC	0.706	261.3 Da LogP -1.51 TPSA 155.7	✓ Ro5	✓ Clean	`NCCC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC104057557 ZINC	0.704	378.2 Da LogP 2.26 TPSA 209.9	✓ Ro5	✓ Clean	`O=C(c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1)c1cc([…`
ZINC1530296 ZINC	0.700	247.2 Da LogP -0.71 TPSA 141.0	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC6783254 ZINC	0.697	231.2 Da LogP 0.61 TPSA 103.7	✓ Ro5	✓ Clean	`CCCC[C@H](NC(=O)CCC(=O)O)C(=O)O`
ZINC6783285 ZINC	0.697	231.2 Da LogP 0.61 TPSA 103.7	✓ Ro5	✓ Clean	`CCCC[C@@H](NC(=O)CCC(=O)O)C(=O)O`
ZINC3080634 ZINC	0.696	200.1 Da LogP 0.91 TPSA 126.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(O)cc([N+](=O)[O-])c1O`
ZINC43450378 ZINC	0.696	366.2 Da LogP 2.40 TPSA 213.0	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(-c2cc([N+](=O)[O-])c(O)c([N+](…`
ZINC1841206 ZINC	0.679	212.1 Da LogP 1.02 TPSA 123.6	✓ Ro5	✓ Clean	`O=Cc1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC32250330 ZINC	0.679	214.1 Da LogP 0.70 TPSA 126.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(CO)c(O)c([N+](=O)[O-])c1`
ZINC5956205 ZINC	0.679	212.2 Da LogP 1.77 TPSA 106.5	✓ Ro5	✓ Clean	`CCc1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC100924232 ZINC	0.667	292.0 Da LogP 2.17 TPSA 129.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc([N+](=O)[O-])c(Br)c([N+](=O)[O…`
ZINC141957116 ZINC	0.667	342.5 Da LogP 4.00 TPSA 92.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)N[C@@H](CCCN)C(=O)O`
ZINC1737586 ZINC	0.667	242.1 Da LogP 1.00 TPSA 132.8	✓ Ro5	✓ Clean	`COC(=O)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC3161143 ZINC	0.667	255.2 Da LogP 0.91 TPSA 126.8	✓ Ro5	✓ Clean	`CN(C)C(=O)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC3161144 ZINC	0.667	241.2 Da LogP 0.57 TPSA 135.6	✓ Ro5	✓ Clean	`CNC(=O)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC78044048 ZINC	0.667	342.5 Da LogP 4.00 TPSA 92.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)N[C@H](CCCN)C(=O)O`
ZINC1655733 ZINC	0.655	240.2 Da LogP 2.51 TPSA 106.5	✓ Ro5	✓ Clean	`CC(C)(C)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC1687159 ZINC	0.655	226.2 Da LogP 2.33 TPSA 106.5	✓ Ro5	✓ Clean	`CC(C)c1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC4343573 ZINC	0.655	214.1 Da LogP 1.22 TPSA 115.7	✓ Ro5	✓ Clean	`COc1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC59195086 ZINC	0.655	242.1 Da LogP 0.84 TPSA 143.8	✓ Ro5	✓ Clean	`O=C(O)Cc1cc([N+](=O)[O-])cc([N+](=O)[O-])c1O`
ZINC104179173 ZINC	0.652	424.2 Da LogP 2.80 TPSA 258.8	1 viol.	✓ Clean	`O=[N+]([O-])c1cc([N+](=O)[O-])c(-c2c([N+](=O)[O…`
ZINC2149898 ZINC	0.652	216.1 Da LogP 0.62 TPSA 147.0	✓ Ro5	Alert	`O=[N+]([O-])c1cc([N+](=O)[O-])c(O)c(O)c1O`
ZINC3593496 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC1529628 ZINC	0.649	274.3 Da LogP -1.32 TPSA 165.6	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NC(=O)CCC(=O)O)C(=O)O`
ZINC3156562 ZINC	0.645	283.2 Da LogP 1.74 TPSA 135.6	✓ Ro5	✓ Clean	`CC(C)(C)NC(=O)c1cc([N+](=O)[O-])cc([N+](=O)[O-]…`
ZINC66139505 ZINC	0.643	305.2 Da LogP 2.78 TPSA 149.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(-c2cc([N+](=O)[O-])c(O)c([N+]…`
ZINC104122301 ZINC	0.640	454.2 Da LogP 2.57 TPSA 282.9	1 viol.	✓ Clean	`O=[N+]([O-])c1cc([N+](=O)[O-])c(NNc2c([N+](=O)[…`
ZINC1693336 ZINC	0.640	218.6 Da LogP 1.86 TPSA 106.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(Cl)cc([N+](=O)[O-])c1O`
ZINC1706150 ZINC	0.640	202.1 Da LogP 1.35 TPSA 106.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(F)cc([N+](=O)[O-])c1O`
ZINC34328127 ZINC	0.640	263.0 Da LogP 1.97 TPSA 106.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(Br)cc([N+](=O)[O-])c1O`
ZINC5113904 ZINC	0.639	261.3 Da LogP -1.51 TPSA 155.7	✓ Ro5	✓ Clean	`NCCC[C@H](NC(=O)[C@@H](N)CCC(=O)O)C(=O)O`
ZINC147300883 ZINC	0.636	217.2 Da LogP 0.22 TPSA 103.7	✓ Ro5	✓ Clean	`CCC[C@@H](NC(=O)CCC(=O)O)C(=O)O`
ZINC24803120 ZINC	0.636	217.2 Da LogP 0.22 TPSA 103.7	✓ Ro5	✓ Clean	`CCC[C@H](NC(=O)CCC(=O)O)C(=O)O`
ZINC100006785 ZINC	0.630	256.1 Da LogP 0.51 TPSA 172.5	✓ Ro5	✓ Clean	`NC(=O)c1c([N+](=O)[O-])cc([N+](=O)[O-])cc1[N+](…`
ZINC116981435 ZINC	0.629	319.3 Da LogP -0.81 TPSA 179.0	1 viol.	✓ Clean	`NCCCC[C@@H](NC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC116981437 ZINC	0.629	319.3 Da LogP -0.81 TPSA 179.0	1 viol.	✓ Clean	`NCCCC[C@@H](NC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC116981440 ZINC	0.629	319.3 Da LogP -0.81 TPSA 179.0	1 viol.	✓ Clean	`NCCCC[C@H](NC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC40860752 ZINC	0.629	319.3 Da LogP -0.81 TPSA 179.0	1 viol.	✓ Clean	`NCCCC[C@H](NC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`

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 A0A0H3H3Z1

Chemistry

ChEMBL CHEMBL330129