KpKP13 Protein target profile

Protocatechuate 3,4-dioxygenase alpha chain

Accession: KP13_04441

Gene: AHE44314.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GP30

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Length 206

Pocket druggability (P2Rank · AlphaFold DB model) 0.094

Direct ligand evidence 0 68 total records

Functional annotation 0 EC 7 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

No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.54. This supports review but is not experimental validation. 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: No hit
Gut microbiome similarity: 0.8% 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: 96.77 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) 0.094

Structure A0A0H3GP30

Pocket Pocket 1

Druggability (FPocket) 0.538

Structure A0A0H3GP30

Pocket Pocket 1

ColabFold model

P2Rank 0.091 · Pocket 1

FPocket 0.527 · Pocket 8

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 37 / 4744 genomes with a hit

Prevalence 0.8%

Sequence

Primary amino-acid sequence viewer.

MKEYLPETASQTAGPYVHIGLAPDAAGFHIFEKNFGPVLTTADTAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPDDRQQQKAVDPAFRGWGRTCSDFTSGIWRFETIKPGPVAGRDGRLMAPHVNLWVVARGINIGLNTRMYFADEHEANASDPVLNLIEWEVRRKTLIAEREVRGTEVVYRFDIHLQGENETVFFDI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0016702 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from one donor, and two oxygen atoms is incorporated into a donor.
GO:0018578 Catalysis of the reaction: 3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate.
GO:0019439 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of aromatic compounds, any substance containing an aromatic carbon ring.
GO:0006725 OBSOLETE. The chemical reactions and pathways involving aromatic compounds, any organic compound characterized by one or more planar rings, each of which contains conjugated double bonds and delocalized pi electrons, as carried out by individual cells.
GO:0005506 Binding to an iron (Fe) ion.
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:0008199 Binding to a ferric iron ion, Fe(III).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

13 records

Show feature table

Start	End	DB	Term	Name
1	206	Gene3D	G3DSA:2.60.130.10	Aromatic compound dioxygenase
1	206	InterPro	IPR015889	Intradiol ring-cleavage dioxygenase, core
5	205	PANTHER	PTHR33711	DIOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02910)-RELATED
5	205	CDD	cd03463	3,4-PCD_alpha
5	205	InterPro	IPR012786	Protocatechuate 3,4-dioxygenase, alpha subunit
42	196	Pfam	PF00775	Dioxygenase
42	196	InterPro	IPR000627	Intradiol ring-cleavage dioxygenase, C-terminal
8	206	NCBIfam	TIGR02423	protocatechuate 3,4-dioxygenase subunit alpha
8	206	InterPro	IPR012786	Protocatechuate 3,4-dioxygenase, alpha subunit
3	206	SUPERFAMILY	SSF49482	Aromatic compound dioxygenase
3	206	InterPro	IPR015889	Intradiol ring-cleavage dioxygenase, core
51	79	ProSitePatterns	PS00083	Intradiol ring-cleavage dioxygenases signature.
51	79	InterPro	IPR000627	Intradiol ring-cleavage dioxygenase, C-terminal

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

0.094

Likely same site as FPocket 1 3.9 Å 8 shared residues 73% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.088

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Surrounding area

Pocket 3 P2Rank #3

0.007

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Surrounding area

Pocket 4 P2Rank #4

0.004

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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 #1

0.538

Likely same site as P2Rank 1 3.9 Å 8 shared residues 73% of smaller site

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Surrounding area

Pocket 2 FPocket #11

0.499

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Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.091

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Surrounding area

Pocket 2 P2Rank #2

0.083

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Surrounding area

Pocket 3 P2Rank #3

0.019

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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_A0A0H3GP30	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04441	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.

68 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 18 records from similar proteins

Structural ligands 18 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3HB PDB via homolog 138.1 Da · LogP 1.09 · TPSA 57.5 Open detail RCSB PDB

3HP PDB via homolog Detail RCSB PDB

3N8 PDB via homolog Detail RCSB PDB

3N9 PDB via homolog Detail RCSB PDB

3NJ 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
3HB RCSB PDB	3PCB	P00437	138.1 Da LogP 1.09 TPSA 57.5	✓ Ro5	✓ Clean	`c1cc(cc(c1)O)C(=O)O`
3HP RCSB PDB	3PCE	P00436	152.1 Da LogP 1.02 TPSA 57.5	✓ Ro5	✓ Clean	`c1cc(cc(c1)O)CC(=O)O`
3N8 RCSB PDB	4WHQ	P00437	128.1 Da LogP 1.24 TPSA 40.5	✓ Ro5	Alert	`c1cc(c(cc1F)O)O`
3N9 RCSB PDB	4WHQ	P00437	160.1 Da LogP 0.16 TPSA 66.8	✓ Ro5	✓ Clean	`C1=CC(=O)[C@@](C=C1F)(O)OO`
3NJ RCSB PDB	4WHR	P00437	142.1 Da LogP 0.14 TPSA 47.3	✓ Ro5	✓ Clean	`C1=CC(=O)OC(=O)C=C1F`
4HP RCSB PDB	3PCG	P00437	152.1 Da LogP 1.02 TPSA 57.5	✓ Ro5	✓ Clean	`c1cc(ccc1CC(=O)O)O`
4NC RCSB PDB	3LXV	P00437	155.1 Da LogP 1.01 TPSA 83.6	✓ Ro5	Alert	`c1cc(c(cc1[N+](=O)[O-])O)O`
CAQ RCSB PDB	3MI5	P00437	110.1 Da LogP 1.10 TPSA 40.5	✓ Ro5	Alert	`c1ccc(c(c1)O)O`
CHB RCSB PDB	3PCH	P00437	172.6 Da LogP 1.74 TPSA 57.5	✓ Ro5	✓ Clean	`c1cc(c(cc1C(=O)O)Cl)O`
DHB RCSB PDB	1YKL	P00437	154.1 Da LogP 0.80 TPSA 77.8	✓ Ro5	Alert	`c1cc(c(cc1C(=O)O)O)O`
DHY RCSB PDB	3MFL	P00437	168.1 Da LogP 0.72 TPSA 77.8	✓ Ro5	Alert	`c1cc(c(cc1CC(=O)O)O)O`
FHB RCSB PDB	3PCF	P00437	156.1 Da LogP 1.23 TPSA 57.5	✓ Ro5	✓ Clean	`c1cc(c(cc1C(=O)O)F)O`
IHB RCSB PDB	3PCI	P00437	264.0 Da LogP 1.70 TPSA 57.5	✓ Ro5	✓ Clean	`c1cc(c(cc1C(=O)O)I)O`
INO RCSB PDB	3PCJ	P00437	155.1 Da LogP -0.28 TPSA 84.5	✓ Ro5	✓ Clean	`c1c[n+](c(cc1C(=O)O)O)[O-]`
MUC RCSB PDB	4WHS	P00437	142.1 Da LogP -0.06 TPSA 63.6	✓ Ro5	✓ Clean	`C1=CC(=O)O[C@H]1CC(=O)O`
NNO RCSB PDB	3PCK	P00437	155.1 Da LogP -0.28 TPSA 84.5	✓ Ro5	✓ Clean	`c1cc([n+](cc1C(=O)O)[O-])O`
PHB RCSB PDB	3PCC	P00437	138.1 Da LogP 1.09 TPSA 57.5	✓ Ro5	✓ Clean	`c1cc(ccc1C(=O)O)O`
PTY RCSB PDB	5TD3	A4JR51	734.1 Da LogP 11.67 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCCCC…`

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
ZINC102190506 ZINC	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512 ZINC	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC27416437 ZINC	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364 ZINC	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC389804 ZINC	0.842	214.2 Da LogP 2.76 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc(O)cc2)cc1`
ZINC32002933 ZINC	0.786	228.2 Da LogP 2.69 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)Cc1cccc(-c2cccc(O)c2)c1`
ZINC13544781 ZINC	0.771	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C…`
ZINC13544783 ZINC	0.771	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC13543439 ZINC	0.750	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC13543441 ZINC	0.750	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC102190945 ZINC	0.739	411.5 Da LogP 3.29 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OCCN`
ZINC32840692 ZINC	0.739	425.5 Da LogP 3.68 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OCCN`
ZINC32840693 ZINC	0.739	425.5 Da LogP 3.68 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OCCN`
ZINC32840704 ZINC	0.739	453.6 Da LogP 4.46 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OCCN`
ZINC32840705 ZINC	0.739	453.6 Da LogP 4.46 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OCCN`
ZINC95635984 ZINC	0.739	397.4 Da LogP 2.90 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OCCN`
ZINC102191119 ZINC	0.729	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](O)CO…`
ZINC58649551 ZINC	0.729	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](O)CO)…`
ZINC148781474 ZINC	0.727	274.2 Da LogP 2.16 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc(C(=O)O)cc2O)c(O)c1`
ZINC33246180 ZINC	0.727	242.2 Da LogP 3.51 TPSA 82.2	✓ Ro5	Alert	`O=C(O)c1ccc(N=Nc2ccc(O)cc2)cc1`
ZINC36178999 ZINC	0.727	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC36179002 ZINC	0.727	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC3896282 ZINC	0.727	242.2 Da LogP 3.51 TPSA 82.2	✓ Ro5	Alert	`O=C(O)c1ccc(/N=N/c2ccc(O)cc2)cc1`
ZINC392302 ZINC	0.727	230.2 Da LogP 2.88 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)c1ccc(Oc2ccc(O)cc2)cc1`
ZINC39410336 ZINC	0.727	242.2 Da LogP 2.16 TPSA 74.6	✓ Ro5	Alert	`O=C(C(=O)c1cccc(O)c1)c1cccc(O)c1`
ZINC36019045 ZINC	0.720	276.2 Da LogP 2.58 TPSA 126.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O)c(-c2cc([N+](=O)[O-])ccc2O)…`
ZINC1675321 ZINC	0.714	274.2 Da LogP 1.57 TPSA 115.1	✓ Ro5	Alert	`O=C(C(=O)c1ccc(O)c(O)c1)c1ccc(O)c(O)c1`
ZINC13543394 ZINC	0.708	455.4 Da LogP 2.15 TPSA 171.7	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](N)C(=O)…`
ZINC5820131 ZINC	0.705	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC5820134 ZINC	0.705	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC289893 ZINC	0.696	278.3 Da LogP 1.92 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)c1ccc(S(=O)(=O)c2ccc(O)cc2)cc1`
ZINC33822387 ZINC	0.694	426.5 Da LogP 2.66 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC33822389 ZINC	0.694	426.5 Da LogP 2.66 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCC[N+](C)(C)C)…`
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`
ZINC2566063 ZINC	0.679	231.0 Da LogP 1.78 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(O)c(Br)c1`
ZINC83072638 ZINC	0.679	231.0 Da LogP 1.78 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(Br)c(O)c1`
ZINC96334879 ZINC	0.679	278.0 Da LogP 1.62 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(O)c(I)c1`
ZINC42417744 ZINC	0.677	209.2 Da LogP 0.14 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)Cc1cccc(O)c1`
ZINC114185151 ZINC	0.667	298.2 Da LogP 2.15 TPSA 108.7	✓ Ro5	Alert	`O=C(O)c1ccc(C(=O)C(=O)c2ccc(C(=O)O)cc2)cc1`
ZINC1726237 ZINC	0.667	265.0 Da LogP 1.90 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O)c(I)c1`
ZINC1750322 ZINC	0.667	218.0 Da LogP 2.06 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O)c(Br)c1`
ZINC2924369 ZINC	0.667	242.2 Da LogP 2.16 TPSA 74.6	✓ Ro5	Alert	`O=C(C(=O)c1ccc(O)cc1)c1ccc(O)cc1`
ZINC352067517 ZINC	0.667	205.2 Da LogP 2.16 TPSA 83.6	✓ Ro5	Alert	`O=[N+]([O-])c1ccc2cc(O)c(O)cc2c1`
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`
ZINC60007417 ZINC	0.667	265.0 Da LogP 1.90 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(I)c(O)c1`
ZINC91682324 ZINC	0.667	218.0 Da LogP 2.06 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Br)c(O)c1`
ZINC1501016364 ZINC	0.654	465.6 Da LogP 4.63 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O…`
ZINC32153033 ZINC	0.650	222.2 Da LogP 3.04 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(F)cc1-c1cc(F)ccc1O`
ZINC139174928 ZINC	0.645	228.2 Da LogP 2.69 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(-c2cccc(O)c2)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 A0A0H3GP30