Protein target profile

VK055_0068

dATP pyrophosphohydrolase

Genome: KpATCC43816 Gene: AIK78696.1 ntpA 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GS12

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Length 147

Pocket druggability 0.417

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 53 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

Central metabolic position More central than 88.9% of genes in this genome. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.42. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.88. 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 (%): 30.579 Lower values reduce human off-target concern.
Human E-value: 1.28e-07
Gut microbiome similarity: 2.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 84.828 Higher values support similarity to known essential genes.
DEG E-value: 1.75e-90 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Unknown

Structure confidence

ColabFold pLDDT: 96.0 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 0.417

Structure A0A0H3GS12

Pocket Pocket 1

P2Rank 0.877

Structure A0A0H3GS12

Pocket Pocket 1

ColabFold model

FPocket 0.817 · Pocket 1

P2Rank 0.912 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 122 / 4744 genomes with a hit

Prevalence 2.6%

Cross-references

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

Sequence

UniProt A0A0H3GS12

Pathways

BioCyc RXN0-384

Metabolic context

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

Explore metabolic network

Metabolic context: more central than 88.9% of genes in this genome.

Relative network centrality 88.9% more central than 88.9% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSFKLPVSVLVVIYAEDTKRVLMLQRRDDPAFWQSVTGSLEAGETALQAAAREVKEEVAIDVACEQLTLIDCQRTVEFEIFSHLRHRYAPGVERNTEFWFCLALPHEREITFTEHLAYRWVSATEAAALTKSWSNRQAIEEFVINAA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

GO:0019177 Catalysis of the reaction: dihydroneopterin triphosphate = dihydroneopterin phosphate + diphosphate.
GO:0046656 The chemical reactions and pathways resulting in the formation of folic acid, pteroylglutamic acid.
GO:0008828 Catalysis of the reaction: dATP + H2O = dAMP + H+ + diphosphate.
GO:0004081 Catalysis of the reaction: P(1),P(4)-bis(5'-nucleosyl)tetraphosphate + H2O = NTP + NMP. Acts on bis(5'-guanosyl)-, bis(5'-xanthosyl)-, bis(5'-adenosyl)- and bis(5'-uridyl)-tetraphosphate.
GO:0046872 Binding to a metal ion.
GO:0006167 The chemical reactions and pathways resulting in the formation of AMP, adenosine monophosphate.
GO:0006754 The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
1	147	Gene3D	G3DSA:3.90.79.10	Nucleoside Triphosphate Pyrophosphohydrolase
5	11	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
4	142	PANTHER	PTHR21340	DIADENOSINE 5,5-P1,P4-TETRAPHOSPHATE PYROPHOSPHOHYDROLASE MUTT
1	15	Phobius	SIGNAL_PEPTIDE	Signal peptide region
4	143	ProSiteProfiles	PS51462	Nudix hydrolase domain profile.
4	143	InterPro	IPR000086	NUDIX hydrolase domain
1	4	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
5	141	Pfam	PF00293	NUDIX domain
5	141	InterPro	IPR000086	NUDIX hydrolase domain
12	15	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
3	140	SUPERFAMILY	SSF55811	Nudix
3	140	InterPro	IPR015797	NUDIX hydrolase-like domain superfamily
16	147	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
6	140	CDD	cd04664	Nudix_Hydrolase_7
99	120	PRINTS	PR01404	DATP pyrophosphohydrolase signature
99	120	InterPro	IPR003564	Dihydroneopterin triphosphate diphosphatase
126	139	PRINTS	PR01404	DATP pyrophosphohydrolase signature
126	139	InterPro	IPR003564	Dihydroneopterin triphosphate diphosphatase
71	90	PRINTS	PR01404	DATP pyrophosphohydrolase signature
71	90	InterPro	IPR003564	Dihydroneopterin triphosphate diphosphatase
3	20	PRINTS	PR01404	DATP pyrophosphohydrolase signature
3	20	InterPro	IPR003564	Dihydroneopterin triphosphate diphosphatase
20	41	PRINTS	PR01404	DATP pyrophosphohydrolase signature
20	41	InterPro	IPR003564	Dihydroneopterin triphosphate diphosphatase

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 #1

0.417

Likely same site as P2Rank 1 0.8 Å 23 shared residues 96% of smaller site

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.877

Likely same site as FPocket 1 0.8 Å 23 shared residues 96% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.015

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Surrounding area

Residue sets

UniProt: Binding site:114-114

UniProt: Binding site:132-132

UniProt: Binding site:26-26

UniProt: Binding site:37-37

UniProt: Binding site:4-4

UniProt: Binding site:53-53

UniProt: Binding site:57-57

UniProt: Binding site:78-81

Residue sets

UniProt: Binding site:114-114

UniProt: Binding site:132-132

UniProt: Binding site:26-26

UniProt: Binding site:37-37

UniProt: Binding site:4-4

UniProt: Binding site:53-53

UniProt: Binding site:57-57

UniProt: Binding site:78-81

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_A0A0H3GS12	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0068	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

DPO PDB via homolog 173.9 Da · LogP -3.34 · TPSA 135.6 Open detail RCSB PDB

MGP PDB via homolog Detail RCSB PDB

PPV PDB via homolog Detail RCSB PDB

ZINC15521877 ZINC proposed compound · Tanimoto 0.982 Detail ZINC

ZINC6827739 ZINC proposed compound · Tanimoto 0.692 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
DPO RCSB PDB	4IJX	P50583	173.9 Da LogP -3.34 TPSA 135.6	✓ Ro5	✓ Clean	`[O-]P(=O)([O-])OP(=O)([O-])[O-]`
MGP RCSB PDB	6SCX	Q9BQG2	538.2 Da LogP -2.91 TPSA 290.1	3 viol.	✓ Clean	`C[n+]1cn(c2c1C(=O)NC(=N2)N)[C@H]3[C@@H]([C@@H](…`
PPV RCSB PDB	2O1C	P0AFC0	178.0 Da LogP -0.81 TPSA 124.3	✓ Ro5	✓ Clean	`OP(=O)(O)OP(=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
ZINC15521877 ZINC	0.982	458.2 Da LogP -3.02 TPSA 243.6	2 viol.	✓ Clean	`C[n+]1cn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O…`
ZINC6827739 ZINC	0.692	258.0 Da LogP -0.69 TPSA 170.8	✓ Ro5	✓ Clean	`O=P(O)(O)OP(=O)(O)OP(=O)(O)O`
ZINC12371988 ZINC	0.683	298.3 Da LogP -3.26 TPSA 150.5	✓ Ro5	✓ Clean	`C[n+]1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c2n…`
ZINC12371989 ZINC	0.683	298.3 Da LogP -3.26 TPSA 150.5	✓ Ro5	✓ Clean	`C[n+]1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c2…`
ZINC14591885 ZINC	0.683	298.3 Da LogP -3.26 TPSA 150.5	✓ Ro5	✓ Clean	`C[n+]1cn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c2n…`
ZINC18130229 ZINC	0.683	298.3 Da LogP -3.26 TPSA 150.5	✓ Ro5	✓ Clean	`C[n+]1cn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c2nc…`
ZINC19939880 ZINC	0.683	298.3 Da LogP -3.26 TPSA 150.5	✓ Ro5	✓ Clean	`C[n+]1cn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c2nc…`
ZINC28523740 ZINC	0.683	298.3 Da LogP -3.26 TPSA 150.5	✓ Ro5	✓ Clean	`C[n+]1cn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c2nc(…`
ZINC5893253 ZINC	0.683	298.3 Da LogP -3.26 TPSA 150.5	✓ Ro5	✓ Clean	`C[n+]1cn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c2nc…`
ZINC104869865 ZINC	0.682	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O…`
ZINC12504289 ZINC	0.682	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC34541308 ZINC	0.682	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC35000839 ZINC	0.682	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC45284491 ZINC	0.682	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC80639694 ZINC	0.682	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC8215481 ZINC	0.682	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC32303987 ZINC	0.606	499.2 Da LogP -2.51 TPSA 290.6	2 viol.	✓ Clean	`Nc1nc(=O)n([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)…`
ZINC59066138 ZINC	0.606	499.2 Da LogP -2.51 TPSA 290.6	2 viol.	✓ Clean	`Nc1nc(=O)n([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=…`
ZINC100058967 ZINC	0.594	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@H]3O[C@H](CO[P@](=O)(O)OP(=O)…`
ZINC12504287 ZINC	0.594	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@@H]3O[C@@H](CO[P@@](=O)(O)OP(…`
ZINC12504288 ZINC	0.594	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@H]3O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC31308647 ZINC	0.594	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@@H]3O[C@@H](CO[P@@](=O)(O)OP(…`
ZINC12502055 ZINC	0.591	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC12502057 ZINC	0.591	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC12502058 ZINC	0.591	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13431057 ZINC	0.591	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13431059 ZINC	0.591	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC25726736 ZINC	0.591	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC3861746 ZINC	0.591	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@@](=O)(O)…`
ZINC53683723 ZINC	0.591	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC82142138 ZINC	0.591	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC82142140 ZINC	0.591	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13548083 ZINC	0.583	459.2 Da LogP -2.76 TPSA 241.2	2 viol.	✓ Clean	`CN1CN([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[C…`
ZINC13519607 ZINC	0.582	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)(O)OP…`
ZINC31298140 ZINC	0.582	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC81168754 ZINC	0.582	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC81168756 ZINC	0.582	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC12501413 ZINC	0.574	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC12958448 ZINC	0.574	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC1532555 ZINC	0.574	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC16546189 ZINC	0.574	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC2159505 ZINC	0.574	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3073318 ZINC	0.574	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869963 ZINC	0.574	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869965 ZINC	0.574	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC9334496 ZINC	0.574	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC13431045 ZINC	0.561	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431047 ZINC	0.561	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC33913782 ZINC	0.561	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC8215624 ZINC	0.561	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(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.