KpATCC43816 Protein target profile

4-hydroxyphenylacetate 3-monooxygenase, oxygenase component

Accession: VK055_2659

Gene: AIK81253.1 hpaB 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GR70

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Length 520

Pocket druggability (P2Rank · AlphaFold DB model) 0.904

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 53 total records

Functional annotation 1 EC 5 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 95.0% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. 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: No hit
Gut microbiome similarity: 1.2% 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: 96.68 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) 0.904

Structure A0A0H3GR70

Pocket Pocket 1

Druggability (FPocket) 0.876

Structure A0A0H3GR70

Pocket Pocket 29

ColabFold model

P2Rank 0.615 · Pocket 1

FPocket 0.972 · Pocket 23

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 55 / 4744 genomes with a hit

Prevalence 1.2%

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, no isoenzyme backup detected, more central than 95.0% of genes in this genome, no human homolog detected.

Relative network centrality 95.0% more central than 95.0% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MKPEDFRADAKRPLTGEEYLKSLQDGREIYIYGERVKDVTTHPAFRNAAASVAQLYDALHKPEMQDSLCWGTDTGSGGYTHKFFRVAKSADDLRQQRDAIAEWSRLSYGWMGRTPDYKAAFGCALGANPAFYGQFEQNARNWYTRIQETGLYFNHAIVNPPIDRHKPADEVKDVYIKLEKETDAGIIVSGAKVVATNSALTHYNMIGFGSAQVMGENPDFALMFVAPMDAEGVKLISRASYEMVAGATGSPYDYPLSSRFDENDAILVMDKVLIPWENVLIYRDFDRCRRWTMEGGFARMYPLQACVRLAVKLDFITALLKRSLECTGTLEFRGVQADLGEVVAWRNMFWALSDSMCSEATPWVNGAWLPAHAALQTYRVMAPMAYAKIKNIIERNVTSGLIYLPSSARDLNNPQIDQYLAKYVRGSNGMDHVERIKILKLMWDAIGSEFGGRHELYEINYSGSQDEIRLQCLRQAQSSGNMDKMMAMVDRCLSEYDQNGWTVPHLHNNADINMLDKLLK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

1.14.14.9

Gene Ontology (GO)

GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
GO:0010124 The chemical reactions and pathways resulting in the breakdown of phenylacetate.
GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
GO:0016712 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from reduced flavin or flavoprotein and one other donor, and one atom of oxygen is incorporated into one donor.
GO:0052881 Catalysis of the reaction: (4-hydroxyphenyl)acetate + FADH(2) + O2 = 3,4-dihydroxyphenylacetate + FAD + H+ + H2O.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
152	282	Gene3D	G3DSA:2.40.110.10	-
152	282	InterPro	IPR046373	Acyl-CoA oxidase/dehydrogenase, middle domain superfamily
13	282	SUPERFAMILY	SSF56645	Acyl-CoA dehydrogenase NM domain-like
13	282	InterPro	IPR009100	Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily
272	494	SUPERFAMILY	SSF47203	Acyl-CoA dehydrogenase C-terminal domain-like
272	494	InterPro	IPR036250	Acyl-CoA dehydrogenase-like, C-terminal
288	488	Pfam	PF03241	4-hydroxyphenylacetate 3-hydroxylase C terminal
288	488	InterPro	IPR024719	HpaB/PvcC/4-BUDH C-terminal
6	514	PANTHER	PTHR36117	4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE-RELATED
6	514	InterPro	IPR004925	HpaB/PvcC/4-BUDH
11	501	PIRSF	PIRSF000331	HpaA_HpaB
11	501	InterPro	IPR004925	HpaB/PvcC/4-BUDH
285	500	Gene3D	G3DSA:1.20.140.10	-
13	151	FunFam	G3DSA:1.10.3140.10:FF:000001	4-hydroxyphenylacetate 3-monooxygenase oxygenase component
2	520	NCBIfam	TIGR02310	4-hydroxyphenylacetate 3-monooxygenase, oxygenase component
2	520	InterPro	IPR012688	4-hydroxyphenylacetate 3-monooxygenase oxygenase component, gammaproteobacteria
1	518	PIRSF	PIRSF500125	4_HPA_large
1	518	InterPro	IPR024677	4-HPA 3-monooxygenase large component/Pyoverdin chromophore biosynthetic protein
152	282	FunFam	G3DSA:2.40.110.10:FF:000026	4-hydroxyphenylacetate 3-monooxygenase oxygenase component
15	280	Pfam	PF11794	4-hydroxyphenylacetate 3-hydroxylase N terminal
15	280	InterPro	IPR024674	HpaB/PvcC/4-BUDH N-terminal
14	151	Gene3D	G3DSA:1.10.3140.10	-

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

0.904

Likely same site as FPocket 29 5.9 Å 30 shared residues 83% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.064

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Surrounding area

Pocket 3 P2Rank #3

0.032

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Surrounding area

Pocket 4 P2Rank #4

0.021

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Surrounding area

Pocket 5 P2Rank #5

0.01

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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 #29

0.876 Unusual size

Likely same site as P2Rank 1 5.9 Å 30 shared residues 83% of smaller site

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Surrounding area

Pocket 2 FPocket #30

0.743

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Surrounding area

Pocket 3 FPocket #7

0.624 Unusual size

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Surrounding area

Pocket 4 FPocket #27

0.256

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Surrounding area

Residue sets

UniProt: Binding site:155-157

UniProt: Binding site:196-196

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.615

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Surrounding area

Pocket 2 P2Rank #2

0.152

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Surrounding area

Pocket 3 P2Rank #3

0.148

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Surrounding area

Pocket 4 P2Rank #4

0.075

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Surrounding area

Pocket 5 P2Rank #5

0.006

Likely same site as FPocket 23 7.6 Å 5 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 #23

0.972 Unusual size

Likely same site as P2Rank 5 7.6 Å 5 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #11

0.479

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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_A0A0H3GR70	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2659	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

4HP PDB via homolog 152.1 Da · LogP 1.02 · TPSA 57.5 Open detail RCSB PDB

FDA PDB via homolog Detail RCSB PDB

NPO PDB via homolog Detail RCSB PDB

ZINC32222424 ZINC proposed compound · Tanimoto 0.864 Detail ZINC

ZINC1507107 ZINC proposed compound · Tanimoto 0.857 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
4HP RCSB PDB	2YYJ	Q5SJP8	152.1 Da LogP 1.02 TPSA 57.5	✓ Ro5	✓ Clean	`c1cc(ccc1CC(=O)O)O`
FDA RCSB PDB	7E8P	Q53008	787.6 Da LogP -1.75 TPSA 363.3	3 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…`
NPO RCSB PDB	7E8P	Q53008	139.1 Da LogP 1.30 TPSA 63.4	✓ Ro5	✓ Clean	`c1cc(ccc1[N+](=O)[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
ZINC32222424 ZINC	0.864	228.2 Da LogP 2.69 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(-c2ccc(O)cc2)cc1`
ZINC1507107 ZINC	0.857	215.2 Da LogP 2.97 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(-c2ccc(O)cc2)cc1`
ZINC100009138 ZINC	0.750	243.2 Da LogP 3.72 TPSA 88.1	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(/N=N\c2ccc(O)cc2)cc1`
ZINC100009140 ZINC	0.750	243.2 Da LogP 3.72 TPSA 88.1	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(/N=N/c2ccc(O)cc2)cc1`
ZINC13836765 ZINC	0.750	247.3 Da LogP 3.45 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Sc2ccc(O)cc2)cc1`
ZINC189331 ZINC	0.750	279.3 Da LogP 2.13 TPSA 97.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(S(=O)(=O)c2ccc(O)cc2)cc1`
ZINC1911545360 ZINC	0.750	241.2 Da LogP 3.47 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(C=Cc2ccc(O)cc2)cc1`
ZINC225426 ZINC	0.750	241.2 Da LogP 3.47 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(/C=C/c2ccc(O)cc2)cc1`
ZINC254392989 ZINC	0.750	243.2 Da LogP 3.72 TPSA 88.1	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(N=Nc2ccc(O)cc2)cc1`
ZINC33246164 ZINC	0.750	241.2 Da LogP 3.47 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(/C=C\c2ccc(O)cc2)cc1`
ZINC370769 ZINC	0.750	231.2 Da LogP 3.09 TPSA 72.6	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Oc2ccc(O)cc2)cc1`
ZINC38237571 ZINC	0.750	243.2 Da LogP 2.53 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(c1ccc(O)cc1)c1ccc([N+](=O)[O-])cc1`
ZINC8419013 ZINC	0.750	230.2 Da LogP 3.04 TPSA 75.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Nc2ccc(O)cc2)cc1`
ZINC1682664 ZINC	0.682	270.3 Da LogP 2.61 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(-c2ccc(CC(=O)O)cc2)cc1`
ZINC391495 ZINC	0.682	298.3 Da LogP 2.73 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(CCc2ccc(CC(=O)O)cc2)cc1`
ZINC21982756 ZINC	0.667	299.3 Da LogP 2.63 TPSA 69.9	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(N2CCN(c3ccc(O)cc3)CC2)cc1`
ZINC33835370 ZINC	0.667	273.2 Da LogP 2.94 TPSA 104.5	✓ Ro5	✓ Clean	`O=C(Nc1ccc(O)cc1)Nc1ccc([N+](=O)[O-])cc1`
ZINC575442763 ZINC	0.667	314.3 Da LogP 2.66 TPSA 83.8	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(COCc2ccc(CC(=O)O)cc2)cc1`
ZINC33604885 ZINC	0.630	202.2 Da LogP 2.17 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc2cc(O)ccc2c1`
ZINC895813 ZINC	0.630	209.2 Da LogP 0.14 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)Cc1ccc(O)cc1`
ZINC156360 ZINC	0.625	262.0 Da LogP 1.92 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(I)cc1`
ZINC167159 ZINC	0.625	215.0 Da LogP 2.08 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(Br)cc1`
ZINC1604377 ZINC	0.619	320.3 Da LogP 4.84 TPSA 86.3	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(-c2ccc(-c3ccc([N+](=O)[O-])cc…`
ZINC1648209 ZINC	0.619	244.2 Da LogP 3.17 TPSA 86.3	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(-c2ccc([N+](=O)[O-])cc2)cc1`
ZINC2173334 ZINC	0.609	300.2 Da LogP 2.57 TPSA 120.4	✓ Ro5	Alert	`O=C(C(=O)c1ccc([N+](=O)[O-])cc1)c1ccc([N+](=O)[…`
ZINC145787882 ZINC	0.600	259.2 Da LogP 2.52 TPSA 89.7	✓ Ro5	✓ Clean	`O=C(Oc1ccc([N+](=O)[O-])cc1)c1ccc(O)cc1`
ZINC1699472 ZINC	0.600	286.3 Da LogP 2.73 TPSA 83.8	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(Oc2ccc(CC(=O)O)cc2)cc1`
ZINC18036964 ZINC	0.600	242.2 Da LogP 3.05 TPSA 75.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(/C=N/c2ccc(O)cc2)cc1`
ZINC18099346 ZINC	0.600	242.2 Da LogP 3.05 TPSA 75.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(/N=C/c2ccc(O)cc2)cc1`
ZINC225997 ZINC	0.600	258.2 Da LogP 2.55 TPSA 92.5	✓ Ro5	✓ Clean	`O=C(Nc1ccc(O)cc1)c1ccc([N+](=O)[O-])cc1`
ZINC2318 ZINC	0.600	212.2 Da LogP 2.98 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(-c2ccccc2)cc1`
ZINC36019045 ZINC	0.600	276.2 Da LogP 2.58 TPSA 126.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O)c(-c2cc([N+](=O)[O-])ccc2O)…`
ZINC369682 ZINC	0.600	294.3 Da LogP 2.10 TPSA 109.5	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(S(=O)(=O)Nc2ccc(O)cc2)cc1`
ZINC3750843 ZINC	0.600	226.3 Da LogP 2.90 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(Cc2ccccc2)cc1`
ZINC39297153 ZINC	0.600	228.2 Da LogP 2.52 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(Cc1ccc(O)cc1)c1ccc(O)cc1`
ZINC1688116 ZINC	0.583	272.2 Da LogP 2.73 TPSA 103.3	✓ Ro5	✓ Clean	`O=C(c1ccc([N+](=O)[O-])cc1)c1ccc([N+](=O)[O-])c…`
ZINC5731136 ZINC	0.581	278.3 Da LogP 2.44 TPSA 92.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc([S@](=O)Nc2ccc(O)cc2)cc1`
ZINC5731137 ZINC	0.581	278.3 Da LogP 2.44 TPSA 92.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc([S@@](=O)Nc2ccc(O)cc2)cc1`
ZINC1256693 ZINC	0.577	226.3 Da LogP 3.29 TPSA 37.3	✓ Ro5	✓ Clean	`Cc1ccc(-c2ccc(CC(=O)O)cc2)cc1`
ZINC195766543 ZINC	0.577	328.4 Da LogP 1.76 TPSA 74.6	✓ Ro5	✓ Clean	`C[Si](C)(c1ccc(CC(=O)O)cc1)c1ccc(CC(=O)O)cc1`
ZINC220053800 ZINC	0.577	242.3 Da LogP 2.47 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(-c2ccc(CO)cc2)cc1`
ZINC2539986 ZINC	0.571	215.2 Da LogP 2.97 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(-c2cccc(O)c2)cc1`
ZINC33427614 ZINC	0.571	215.2 Da LogP 2.97 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(-c2ccc(O)cc2)c1`
ZINC139174928 ZINC	0.567	228.2 Da LogP 2.69 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(-c2cccc(O)c2)cc1`
ZINC1511626 ZINC	0.565	249.0 Da LogP 2.20 TPSA 43.1	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(I)cc1`
ZINC1666827 ZINC	0.565	202.0 Da LogP 2.36 TPSA 43.1	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Br)cc1`
ZINC4616626 ZINC	0.563	257.2 Da LogP 2.75 TPSA 87.8	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(N/N=C/c2ccc(O)cc2)cc1`
ZINC7718004 ZINC	0.563	269.3 Da LogP 3.20 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccc([N+](=O)[O-])cc1)c1ccc(O)cc1`
ZINC104058859 ZINC	0.560	395.3 Da LogP 3.70 TPSA 149.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(C(O)(c2ccc([N+](=O)[O-])cc2)c…`
ZINC2584252 ZINC	0.560	203.2 Da LogP 0.84 TPSA 97.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(S(=O)(=O)O)cc1`

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 A0A0H3GR70

Pathways

BioCyc RXN-8505