Protein target profile

VK055_0081

glucose-6-phosphate dehydrogenase

Genome: KpATCC43816 Gene: AIK78709.1 zwf 3D evidence: AlphaFold DB model + ColabFold model Metabolism 3 reactions UniProt A0A0H3GQ55

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Length 491

Pocket druggability 0.696

Metabolic reactions 3

Chokepoint Yes

Direct ligand evidence 0 52 total records

Functional annotation 1 EC 6 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 bottleneck Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. 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. Moderate predicted binding pocket FPocket selected-pocket score 0.70. This supports review but is not experimental validation. 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 (%): 38.346 Lower values reduce human off-target concern.
Human E-value: 1.11e-88
Gut microbiome similarity: 2.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 95.723 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 93.49 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.696

Structure A0A0H3GQ55

Pocket Pocket 3

P2Rank 0.538

Structure A0A0H3GQ55

Pocket Pocket 1

ColabFold model

FPocket 0.79 · Pocket 39

P2Rank 0.386 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 118 / 4744 genomes with a hit

Prevalence 2.5%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GQ55

Pathways

BioCyc GLU6PDEHYDROG-RXN-ALPHA-GLC-6-P/NADP//D-6-P-GLUCONO-DELTA-LACTONE/NADPH/PROTON.61. BioCyc GLU6PDEHYDROG-RXN-GLC-6-P/NADP//D-6-P-GLUCONO-DELTA-LACTONE/NADPH/PROTON.55. KEGG R02736 BioCyc GLU6PDEHYDROG-RXN

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 Glutathione metabolism, no isoenzyme backup detected.

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MAVTQTAQACDLVIFGAKGDLARRKLLPSLYQLEKAGQIHADTRIIGVGRADWDKAAYTKVVREALETFMKEKIDEGLWDTLSGRLEFCNLDVNDTSGFTRLGEMLDQKNRVTINYFAMPPSTFGAICKGLGEAKLNAKPARVVMEKPLGTSLETSREINDQVGEFFEECQVYRIDHYLGKETVLNLLALRFANSLFVNNWDCRTIDHVEITVAEEVGIEGRWGYFDQAGQMRDMIQNHLLQILCMIAMSPPSDLSADSIRDEKVKVLKSLRRIDRSNVREKTVRGQYTAGFAQGKKVPGYLEEEGANKTSNTETFVAIRVDIDNWRWAGVPFYLRTGKRLPTKCSEVVVYFKTPELNLFKETWQELPQNKLTIRLQPDEGVDIQVLNKVPGLDHKHNLQITKLDLSYSETFNQTHLADAYERLLLETMRGIQALFVRRDEVEEAWKWVDSITEAWAADRDAPKPYQAGTWGPVASVAMITRDGRSWNEFE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1.1.1.49

Gene Ontology (GO)

GO:0016614 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group act as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
GO:0004345 Catalysis of the reaction: D-glucose 6-phosphate + NADP+ = D-glucono-1,5-lactone 6-phosphate + NADPH + H+.
GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
GO:0006006 The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0009051 The branch of the pentose-phosphate shunt which involves the oxidation of glucose 6-P and produces ribulose 5-P, reduced NADP+ and carbon dioxide (CO2).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

30 records

Show feature table

Start	End	DB	Term	Name
9	489	NCBIfam	TIGR00871	glucose-6-phosphate dehydrogenase
9	489	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
176	182	ProSitePatterns	PS00069	Glucose-6-phosphate dehydrogenase active site.
176	182	InterPro	IPR019796	Glucose-6-phosphate dehydrogenase, active site
176	479	Gene3D	G3DSA:3.30.360.10	Dihydrodipicolinate Reductase; domain 2
1	491	PIRSF	PIRSF000110	G6PD
1	491	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
218	235	PRINTS	PR00079	Glucose-6-phosphate dehydrogenase signature
218	235	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
166	194	PRINTS	PR00079	Glucose-6-phosphate dehydrogenase signature
166	194	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
142	155	PRINTS	PR00079	Glucose-6-phosphate dehydrogenase signature
142	155	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
327	353	PRINTS	PR00079	Glucose-6-phosphate dehydrogenase signature
327	353	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
236	252	PRINTS	PR00079	Glucose-6-phosphate dehydrogenase signature
236	252	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
13	186	Pfam	PF00479	Glucose-6-phosphate dehydrogenase, NAD binding domain
13	186	InterPro	IPR022674	Glucose-6-phosphate dehydrogenase, NAD-binding
5	486	PANTHER	PTHR23429	GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD
5	486	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
9	489	Hamap	MF_00966	Glucose-6-phosphate 1-dehydrogenase [zwf].
12	437	Gene3D	G3DSA:3.40.50.720	-
12	198	FunFam	G3DSA:3.40.50.720:FF:000079	Glucose-6-phosphate 1-dehydrogenase
188	488	Pfam	PF02781	Glucose-6-phosphate dehydrogenase, C-terminal domain
188	488	InterPro	IPR022675	Glucose-6-phosphate dehydrogenase, C-terminal
4	189	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
4	189	InterPro	IPR036291	NAD(P)-binding domain superfamily
176	488	SUPERFAMILY	SSF55347	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
176	479	FunFam	G3DSA:3.30.360.10:FF:000011	Glucose-6-phosphate 1-dehydrogenase

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 · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #3

0.696

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Surrounding area

Site 2 FPocket #46

0.517

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Surrounding area

Site 3 FPocket #28

0.412

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Surrounding area

Site 4 FPocket #17

0.379

Likely same site as P2Rank 3 3.0 Å 8 shared residues 89% of smaller site

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.538

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Surrounding area

Site 2 P2Rank #2

0.063

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Surrounding area

Site 3 P2Rank #3

0.053

Likely same site as FPocket 17 3.0 Å 8 shared residues 89% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.048

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Surrounding area

Site 5 P2Rank #5

0.044

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Surrounding area

Residue sets

UniProt: Active site:239-239 Proton acceptor

UniProt: Binding site:147-147

UniProt: Binding site:177-177

UniProt: Binding site:181-181

UniProt: Binding site:215-215

UniProt: Binding site:234-234

UniProt: Binding site:339-339

UniProt: Binding site:344-344

UniProt: Binding site:50-50

UniProt: Binding site:92-93

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.386

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Surrounding area

Site 2 P2Rank #2

0.084

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Surrounding area

Site 3 P2Rank #3

0.047

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Surrounding area

Site 4 P2Rank #4

0.028

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Surrounding area

Site 5 P2Rank #5

0.017

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Surrounding area

Residue sets

UniProt: Active site:239-239 Proton acceptor

UniProt: Binding site:147-147

UniProt: Binding site:177-177

UniProt: Binding site:181-181

UniProt: Binding site:215-215

UniProt: Binding site:234-234

UniProt: Binding site:339-339

UniProt: Binding site:344-344

UniProt: Binding site:50-50

UniProt: Binding site:92-93

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_A0A0H3GQ55	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0081	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.

52 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 2 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

BG6 PDB via homolog 260.1 Da · LogP -3.10 · TPSA 156.9 Open detail RCSB PDB

GOA PDB via homolog Detail RCSB PDB

ZINC100351935 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC1529564 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC1532533 ZINC proposed compound · Tanimoto 1.000 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
BG6 RCSB PDB	7E6I	P48828	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`C([C@@H]1[C@H]([C@@H]([C@H]([C@@H](O1)O)O)O)O)O…`
GOA RCSB PDB	1QKI	P11413	76.1 Da LogP -0.94 TPSA 57.5	✓ Ro5	✓ Clean	`C(C(=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
ZINC100351935 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@H](O)[C@H](O)[C@@…`
ZINC1529564 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@H](O)[C@H](O)[C@…`
ZINC1532533 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC1532857 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C…`
ZINC3581460 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C…`
ZINC38276879 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC38276880 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@H…`
ZINC3869397 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H](O)[C…`
ZINC3875374 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@…`
ZINC3875375 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@…`
ZINC4095545 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@…`
ZINC4095546 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H…`
ZINC4096188 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@@H](O)[C@…`
ZINC8551507 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC12504154 ZINC	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@@H]1O`
ZINC1532546 ZINC	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H]1O`
ZINC4096190 ZINC	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H]1O`
ZINC4228241 ZINC	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H]1O`
ZINC4521831 ZINC	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H]1O`
ZINC13516910 ZINC	0.733	244.1 Da LogP -2.42 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC2562340 ZINC	0.733	244.1 Da LogP -2.42 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC4097102 ZINC	0.719	259.2 Da LogP -3.14 TPSA 162.7	1 viol.	✓ Clean	`N[C@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC4097103 ZINC	0.719	259.2 Da LogP -3.14 TPSA 162.7	1 viol.	✓ Clean	`N[C@H]1[C@@H](O)O[C@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC12502703 ZINC	0.667	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](OP(=O)(O)O)[C@H](O)[C@…`
ZINC4095589 ZINC	0.667	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](OP(=O)(O)O)[C@H](O)[C@@…`
ZINC15298193 ZINC	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@H…`
ZINC1933262384 ZINC	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@H…`
ZINC1933262385 ZINC	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@H…`
ZINC1933262386 ZINC	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@H]…`
ZINC1933262387 ZINC	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@H]…`
ZINC256073272 ZINC	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@H…`
ZINC256073273 ZINC	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@…`
ZINC256073274 ZINC	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@H…`
ZINC256073275 ZINC	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@…`
ZINC4228300 ZINC	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@H]2O[C@H](CO)[C@@H]…`
ZINC56870785 ZINC	0.656	228.1 Da LogP -1.40 TPSA 116.5	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](O)[C@H]1O`
ZINC13522068 ZINC	0.636	310.1 Da LogP -2.35 TPSA 183.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](OP(=O)(O)O)[C@H](O)[C@@…`
ZINC3870205 ZINC	0.636	310.1 Da LogP -2.35 TPSA 183.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](OP(=O)(O)O)[C@@H](O)[C…`
ZINC4095560 ZINC	0.636	310.1 Da LogP -2.35 TPSA 183.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](OP(=O)(O)O)[C@H](O)[C@…`
ZINC13513381 ZINC	0.622	301.2 Da LogP -2.12 TPSA 169.3	1 viol.	✓ Clean	`C/C(O)=N/[C@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@H]…`
ZINC30725927 ZINC	0.622	301.2 Da LogP -2.12 TPSA 169.3	1 viol.	✓ Clean	`C/C(O)=N/[C@H]1[C@@H](O)O[C@H](COP(=O)(O)O)[C@H…`
ZINC100350901 ZINC	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@H](…`
ZINC1530414 ZINC	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@@H](O)O[C@@H](COP(=O)(O)O)[C@H…`
ZINC1532625 ZINC	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@H]1[C@H](O)[C@@H](O)[C@H](COP(=O)(O)O…`
ZINC245204467 ZINC	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@H]1[C@H](O)[C@@H](O)[C@@H](COP(=O)(O)…`
ZINC245204468 ZINC	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@H]1[C@H](O)[C@H](O)[C@@H](COP(=O)(O)O…`
ZINC30725207 ZINC	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC4096363 ZINC	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@@H](O)O[C@H](COP(=O)(O)O)[C@@H…`
ZINC4097100 ZINC	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@H]1[C@@H](O)O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC4097101 ZINC	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@@H](…`

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.