KpATCC43816 Protein target profile

pyridoxine 5'-phosphate synthase

Accession: VK055_4612

Gene: pdxJ AIK83146.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GTT4

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Length 243

Pocket druggability (P2Rank · AlphaFold DB model) 0.869

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 53 total records

Functional annotation 1 EC 4 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 89.5% 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: 5.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 93.827 Higher values support similarity to known essential genes.
DEG E-value: 8.83e-169 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 96.9 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) 0.869

Structure A0A0H3GTT4

Pocket Pocket 1

Druggability (FPocket) 0.216

Structure A0A0H3GTT4

Pocket Pocket 12

ColabFold model

P2Rank 0.891 · Pocket 1

FPocket 0.571 · Pocket 5

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 271 / 4744 genomes with a hit

Prevalence 5.7%

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a consuming chokepoint reaction in Vitamin B6 metabolism, no isoenzyme backup detected, more central than 89.5% of genes in this genome, no human homolog detected.

Relative network centrality 89.5% more central than 89.5% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MAELLLGVNIDHIATLRNARGTAYPDPVQAAFIAEQAGADGITVHLREDRRHITDRDVRILRQTLHTRMNLEMAVTEEMLTIACETKPHFCCLVPEKRQEVTTEGGLDVAGQRDKMRDACQRLADAGILVSLFIDADQAQIKAAADVGAPYIEIHTGCYADAKTDAEQARELERIAKAATYAASLGLKVNAGHGLTYHNVKAIAALPEMHELNIGHAIIGRAVMSGLKEAVAEMKRLMLEARG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.6.99.2

Gene Ontology (GO)

GO:0033856 Catalysis of the reaction: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = 2 H2O + H+ + phosphate + pyridoxine 5'-phosphate.
GO:0008615 The chemical reactions and pathways resulting in the formation of pyridoxine, 2-methyl-3-hydroxy-4,5-bis(hydroxymethyl)pyridine, one of the vitamin B6 compounds.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

15 records

Show feature table

Start	End	DB	Term	Name
6	238	Pfam	PF03740	Pyridoxal phosphate biosynthesis protein PdxJ
6	238	InterPro	IPR004569	Pyridoxal phosphate (active vitamin B6) biosynthesis PdxJ
4	242	PANTHER	PTHR30456	PYRIDOXINE 5'-PHOSPHATE SYNTHASE
4	242	InterPro	IPR004569	Pyridoxal phosphate (active vitamin B6) biosynthesis PdxJ
1	243	FunFam	G3DSA:3.20.20.70:FF:000042	Pyridoxine 5'-phosphate synthase
6	239	NCBIfam	TIGR00559	pyridoxine 5'-phosphate synthase
6	239	InterPro	IPR004569	Pyridoxal phosphate (active vitamin B6) biosynthesis PdxJ
1	243	Hamap	MF_00279	Pyridoxine 5'-phosphate synthase [pdxJ].
1	243	InterPro	IPR004569	Pyridoxal phosphate (active vitamin B6) biosynthesis PdxJ
5	238	CDD	cd00003	PNPsynthase
5	238	InterPro	IPR004569	Pyridoxal phosphate (active vitamin B6) biosynthesis PdxJ
1	243	Gene3D	G3DSA:3.20.20.70	Aldolase class I
1	243	InterPro	IPR013785	Aldolase-type TIM barrel
4	241	SUPERFAMILY	SSF63892	Pyridoxine 5'-phosphate synthase
4	241	InterPro	IPR036130	Pyridoxine 5'-phosphate synthase

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

0.869

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Surrounding area

Pocket 2 P2Rank #2

0.058

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Surrounding area

Pocket 3 P2Rank #3

0.032

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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 #12

0.216

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Surrounding area

Residue sets

UniProt: Active site:193-193 Proton donor

UniProt: Active site:45-45 Proton acceptor

UniProt: Active site:72-72 Proton acceptor

UniProt: Binding site:102-102

UniProt: Binding site:11-12

UniProt: Binding site:194-194

UniProt: Binding site:20-20

UniProt: Binding site:215-216

UniProt: Binding site:47-47

UniProt: Binding site:52-52

UniProt: Binding site:9-9

UniProt: Site:153-153 Transition state stabilizer

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.891

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Surrounding area

Pocket 2 P2Rank #2

0.038

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Surrounding area

Pocket 3 P2Rank #3

0.034

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Surrounding area

Pocket 4 P2Rank #4

0.013

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Surrounding area

Pocket 5 P2Rank #5

0.006

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Surrounding area

Residue sets

UniProt: Active site:193-193 Proton donor

UniProt: Active site:45-45 Proton acceptor

UniProt: Active site:72-72 Proton acceptor

UniProt: Binding site:102-102

UniProt: Binding site:11-12

UniProt: Binding site:194-194

UniProt: Binding site:20-20

UniProt: Binding site:215-216

UniProt: Binding site:47-47

UniProt: Binding site:52-52

UniProt: Binding site:9-9

UniProt: Site:153-153 Transition state stabilizer

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_A0A0H3GTT4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4612	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

DXP PDB via homolog 214.1 Da · LogP -1.59 · TPSA 124.3 Open detail RCSB PDB

G3P PDB via homolog Detail RCSB PDB

PXP PDB via homolog Detail RCSB PDB

ZINC1532705 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC1532708 ZINC proposed compound · Tanimoto 0.769 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
DXP RCSB PDB	1IXN	P0A794	214.1 Da LogP -1.59 TPSA 124.3	✓ Ro5	✓ Clean	`CC(=O)[C@H]([C@@H](COP(=O)(O)O)O)O`
G3P RCSB PDB	1IXN	P0A794	172.1 Da LogP -1.55 TPSA 107.2	✓ Ro5	✓ Clean	`C([C@H](COP(=O)(O)O)O)O`
PXP RCSB PDB	1HO4	P0A794	249.2 Da LogP 0.20 TPSA 120.1	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CO)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
ZINC1532705 ZINC	1.000	249.2 Da LogP 0.20 TPSA 120.1	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CO)c1O`
ZINC1532708 ZINC	0.769	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CN)c1O`
ZINC1529618 ZINC	0.739	246.2 Da LogP -2.17 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(OC[C@@H](O)CO)OC[C@H](O)CO`
ZINC1529620 ZINC	0.739	246.2 Da LogP -2.17 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(OC[C@@H](O)CO)OC[C@@H](O)CO`
ZINC1656021 ZINC	0.711	233.2 Da LogP 1.01 TPSA 99.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(C)c1O`
ZINC1532514 ZINC	0.659	247.1 Da LogP 0.52 TPSA 117.0	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(C=O)c1O`
ZINC5975509 ZINC	0.640	202.1 Da LogP -2.19 TPSA 127.5	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H](O)[C@H](O)CO`
ZINC1529626 ZINC	0.633	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC1532567 ZINC	0.633	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC1532851 ZINC	0.633	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC30320708 ZINC	0.633	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC3870277 ZINC	0.633	310.1 Da LogP -2.50 TPSA 191.0	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC5830339 ZINC	0.613	231.1 Da LogP -2.68 TPSA 156.5	1 viol.	✓ Clean	`O=C(NO)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC2516111 ZINC	0.593	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)CO`
ZINC2522704 ZINC	0.593	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC3869812 ZINC	0.593	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC1842949 ZINC	0.578	243.2 Da LogP -0.49 TPSA 120.1	✓ Ro5	✓ Clean	`Cc1ncc(CO[C@@H](O)C(=O)O)c(CO)c1O`
ZINC639 ZINC	0.578	243.2 Da LogP -0.49 TPSA 120.1	✓ Ro5	✓ Clean	`Cc1ncc(CO[C@H](O)C(=O)O)c(CO)c1O`
ZINC4095590 ZINC	0.567	215.1 Da LogP -1.57 TPSA 122.2	✓ Ro5	✓ Clean	`NCCO[P@@](=O)(O)OC[C@H](O)CO`
ZINC4095591 ZINC	0.567	215.1 Da LogP -1.57 TPSA 122.2	✓ Ro5	✓ Clean	`NCCO[P@@](=O)(O)OC[C@@H](O)CO`
ZINC12501558 ZINC	0.563	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(…`
ZINC12501560 ZINC	0.563	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O…`
ZINC12501562 ZINC	0.563	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)…`
ZINC12501564 ZINC	0.563	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(…`
ZINC1532623 ZINC	0.563	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(…`
ZINC2047359 ZINC	0.563	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)COP(=O…`
ZINC2545091 ZINC	0.563	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O…`
ZINC3869602 ZINC	0.563	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)COP(=…`
ZINC3869603 ZINC	0.563	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)COP(=O…`
ZINC3869604 ZINC	0.563	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)…`
ZINC100065511 ZINC	0.545	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC100085043 ZINC	0.545	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC104869937 ZINC	0.545	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC12502210 ZINC	0.545	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)[C@@H](O)COP(=O…`
ZINC12502212 ZINC	0.545	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)[C@H](O)COP(=O)…`
ZINC12502214 ZINC	0.545	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@@H](O)[C@@H](O)COP(=…`
ZINC12502216 ZINC	0.545	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@@H](O)[C@H](O)COP(=O…`
ZINC13537943 ZINC	0.545	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC4523251 ZINC	0.545	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@@H](O)[C@@H](O)COP(…`
ZINC4523255 ZINC	0.545	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@@H](O)[C@H](O)COP(=…`
ZINC4523257 ZINC	0.545	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@H](O)[C@@H](O)COP(=…`
ZINC4523259 ZINC	0.545	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@H](O)[C@H](O)COP(=O…`
ZINC85994845 ZINC	0.545	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC1680142 ZINC	0.533	212.1 Da LogP -0.34 TPSA 96.2	✓ Ro5	✓ Clean	`C=CCOC[C@@H](O)COP(=O)(O)O`
ZINC5426687 ZINC	0.533	212.1 Da LogP -0.34 TPSA 96.2	✓ Ro5	✓ Clean	`C=CCOC[C@H](O)COP(=O)(O)O`
ZINC100067589 ZINC	0.531	334.2 Da LogP -4.34 TPSA 197.4	1 viol.	✓ Clean	`O=[P@@](O)(OC[C@H](O)CO)O[C@H]1[C@H](O)[C@@H](O…`
ZINC100620818 ZINC	0.531	334.2 Da LogP -4.34 TPSA 197.4	1 viol.	✓ Clean	`O=[P@@](O)(OC[C@H](O)CO)O[C@H]1[C@@H](O)[C@@H](…`
ZINC2384698 ZINC	0.531	244.2 Da LogP -0.14 TPSA 105.5	✓ Ro5	✓ Clean	`CCOC(OCC)[C@H](O)COP(=O)(O)O`
ZINC4521532 ZINC	0.531	244.2 Da LogP -0.14 TPSA 105.5	✓ Ro5	✓ Clean	`CCOC(OCC)[C@@H](O)COP(=O)(O)O`
ZINC5132038 ZINC	0.529	290.2 Da LogP -3.90 TPSA 185.0	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)COP(=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 A0A0H3GTT4

Pathways

KEGG R05838 BioCyc PDXJ-RXN