KpATCC43816 Protein target profile

purine nucleoside phosphorylase

Accession: VK055_2591

Gene: AIK81188.1 deoD 3D evidence: AlphaFold DB model + ColabFold model Metabolism 8 reactions UniProt A0A0H3GM89

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Length 230

Pocket druggability (P2Rank · AlphaFold DB model) 0.797

Metabolic reactions 8

Chokepoint Yes

Direct ligand evidence 0 76 total records

Functional annotation 1 EC 8 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 98.2% 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: 16.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 43.243 Higher values support similarity to known essential genes.
DEG E-value: 8.41e-55 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.1 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) 0.797

Structure A0A0H3GM89

Pocket Pocket 1

Druggability (FPocket) 0.684

Structure A0A0H3GM89

Pocket Pocket 6

ColabFold model

P2Rank 0.55 · Pocket 1

FPocket 0.883 · Pocket 3

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 765 / 4744 genomes with a hit

Prevalence 16.1%

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 Cysteine and methionine metabolism, no isoenzyme backup detected, more central than 98.2% of genes in this genome, no human homolog detected.

Relative network centrality 98.2% more central than 98.2% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MGDFADVVLMPGDPLRAKHIAETFLEDVREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVREDVKLRDVVIGMGACTDSKVNRLRFKDHDFAAIADFGMVRNAVDAAKALGVDARVGNIFSVDLLYTPDPSMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDKE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.4.2.1

Gene Ontology (GO)

GO:0016763 Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor).
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:0009116 The chemical reactions and pathways involving a nucleoside, a nucleobase linked to either beta-D-ribofuranose (a ribonucleoside) or 2-deoxy-beta-D-ribofuranose, (a deoxyribonucleoside), e.g. adenosine, guanosine, inosine, cytidine, uridine and deoxyadenosine, deoxyguanosine, deoxycytidine and thymidine (= deoxythymidine).
GO:0004731 Catalysis of the reaction: purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate.
GO:0006139 Any cellular metabolic process involving nucleobases, nucleosides, nucleotides and nucleic acids.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0047975 Catalysis of the reaction: guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine.
GO:0006152 The chemical reactions and pathways resulting in the breakdown of purine nucleoside, one of a family of organic molecules consisting of a purine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
2	225	SUPERFAMILY	SSF53167	Purine and uridine phosphorylases
2	225	InterPro	IPR035994	Nucleoside phosphorylase superfamily
1	225	NCBIfam	TIGR00107	purine-nucleoside phosphorylase
1	225	InterPro	IPR004402	Purine nucleoside phosphorylase DeoD-type
6	211	Pfam	PF01048	Phosphorylase superfamily
6	211	InterPro	IPR000845	Nucleoside phosphorylase domain
1	226	Hamap	MF_01627	Purine nucleoside phosphorylase DeoD-type [deoD].
1	226	InterPro	IPR004402	Purine nucleoside phosphorylase DeoD-type
1	229	Gene3D	G3DSA:3.40.50.1580	Nucleoside phosphorylase domain
1	229	InterPro	IPR035994	Nucleoside phosphorylase superfamily
225	230	Coils	Coil	Coil
2	223	CDD	cd09006	PNP_EcPNPI-like
2	223	InterPro	IPR004402	Purine nucleoside phosphorylase DeoD-type
53	68	ProSitePatterns	PS01232	Purine and other phosphorylases family 1 signature.
53	68	InterPro	IPR018016	Nucleoside phosphorylase, conserved site
2	223	PANTHER	PTHR43691	URIDINE PHOSPHORYLASE
1	226	FunFam	G3DSA:3.40.50.1580:FF:000002	Purine nucleoside phosphorylase DeoD-type

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

0.797

Likely same site as FPocket 6 1.4 Å 26 shared residues 96% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.082

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Surrounding area

Pocket 3 P2Rank #3

0.016

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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 #6

0.684 Unusual size

Likely same site as P2Rank 1 1.4 Å 26 shared residues 96% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:205-205 Proton donor

UniProt: Binding site:180-182 in other chain

UniProt: Binding site:204-205 in other chain

UniProt: Binding site:21-21 in other chain

UniProt: Binding site:25-25 in other chain

UniProt: Binding site:44-44

UniProt: Binding site:5-5

UniProt: Binding site:88-91 in other chain

UniProt: Site:218-218 Important for catalytic activity

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.55

Likely same site as FPocket 3 5.2 Å 15 shared residues 94% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.209

Likely same site as FPocket 3 5.9 Å 17 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.065

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Surrounding area

Pocket 4 P2Rank #4

0.012

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Surrounding area

Pocket 5 P2Rank #5

0.002

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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 #3

0.883 Unusual size

Likely same site as P2Rank 1 5.2 Å 15 shared residues 94% of smaller site

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Surrounding area

Pocket 2 FPocket #2

0.414

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Surrounding area

Residue sets

UniProt: Active site:205-205 Proton donor

UniProt: Binding site:180-182 in other chain

UniProt: Binding site:204-205 in other chain

UniProt: Binding site:21-21 in other chain

UniProt: Binding site:25-25 in other chain

UniProt: Binding site:44-44

UniProt: Binding site:88-91 in other chain

UniProt: Site:218-218 Important for catalytic activity

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_A0A0H3GM89	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2591	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.

76 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 26 records from similar proteins

Structural ligands 26 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

223 PDB via homolog 263.3 Da · LogP -0.67 · TPSA 111.3 Open detail RCSB PDB

2FA PDB via homolog Detail RCSB PDB

2FD PDB via homolog Detail RCSB PDB

6CR PDB via homolog Detail RCSB PDB

6MP 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
223 RCSB PDB	2ISC	A2E7Y6	263.3 Da LogP -0.67 TPSA 111.3	✓ Ro5	✓ Clean	`c1c(c2c([nH]1)c(ncn2)N)C[N@@]3C[C@@H]([C@H](C3)…`
2FA RCSB PDB	1PK9	P0ABP9	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`c1nc2c(nc(nc2n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO)…`
2FD RCSB PDB	1PKE	P0ABP9	269.2 Da LogP -0.81 TPSA 119.3	✓ Ro5	✓ Clean	`c1nc2c(nc(nc2n1[C@H]3C[C@@H]([C@H](O3)CO)O)F)N`
6CR RCSB PDB	4DAE	O34925	301.7 Da LogP -1.33 TPSA 139.5	✓ Ro5	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO)O)O)nc…`
6MP RCSB PDB	1OTY	P0ABP8	134.1 Da LogP 0.66 TPSA 54.5	✓ Ro5	✓ Clean	`Cc1c2c(nc[nH]2)ncn1`
7HX RCSB PDB	5IU6	P0ABP8	135.1 Da LogP 0.66 TPSA 61.8	✓ Ro5	✓ Clean	`c1c[nH]c2c1c(ncn2)O`
AC2 RCSB PDB	5I3C	A7ZVS7	225.2 Da LogP -1.33 TPSA 119.0	✓ Ro5	✓ Clean	`c1nc2c(n1COCCO)N=C(NC2=O)N`
ADE RCSB PDB	4D8V	O34925	135.1 Da LogP -0.06 TPSA 80.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)c(ncn2)N`
ADN RCSB PDB	1PK7	P0ABP9	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
BG2 RCSB PDB	4DA8	O34925	362.1 Da LogP -1.92 TPSA 159.5	✓ Ro5	✓ Clean	`C([C@@H]1[C@H]([C@H]([C@@H](O1)n2c3c(nc2Br)C(=O…`
DBM RCSB PDB	1OV6	P0ABP8	280.3 Da LogP -0.87 TPSA 113.5	✓ Ro5	✓ Clean	`Cc1c2c(ncn1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
DIH RCSB PDB	3OCC	B1JL34	265.3 Da LogP -2.38 TPSA 106.4	✓ Ro5	✓ Clean	`c1c(c2c([nH]1)C(=O)NC=N2)C[NH+]3C[C@@H]([C@H](C…`
FM1 RCSB PDB	1K9S	P0ABP8	281.3 Da LogP -1.45 TPSA 136.4	✓ Ro5	✓ Clean	`CNc1c2c(c(n[nH]2)[C@H]3[C@@H]([C@@H]([C@H](O3)C…`
FM2 RCSB PDB	1K9S	P0ABP8	282.3 Da LogP -2.48 TPSA 141.4	✓ Ro5	✓ Clean	`C[n+]1cnc2c(c1N)[nH]nc2[C@H]3[C@@H]([C@@H]([C@H…`
FMB RCSB PDB	1A69	P0ABP8	268.2 Da LogP -2.20 TPSA 144.4	✓ Ro5	✓ Clean	`C1=Nc2c(n[nH]c2C(=O)N1)[C@H]3[C@@H]([C@@H]([C@H…`
FMC RCSB PDB	3UT6	P0ABP8	267.2 Da LogP -1.91 TPSA 150.4	✓ Ro5	✓ Clean	`c1nc2c(c(n1)N)[nH]nc2[C@H]3[C@@H]([C@@H]([C@H](…`
GA2 RCSB PDB	4DA6	O34925	255.2 Da LogP -1.97 TPSA 139.3	✓ Ro5	✓ Clean	`c1nc2c(n1COC(CO)CO)N=C(NC2=O)N`
HPA RCSB PDB	5MX6	P56463	136.1 Da LogP -0.35 TPSA 74.4	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)N=CNC2=O`
MDR RCSB PDB	1OVG	P0ABP8	250.3 Da LogP -0.22 TPSA 93.3	✓ Ro5	✓ Clean	`Cc1c2c(ncn1)n(cn2)[C@H]3C[C@@H]([C@H](O3)CO)O`
MTP RCSB PDB	1PR4	P0ABP9	298.3 Da LogP -0.84 TPSA 113.5	✓ Ro5	✓ Clean	`CSc1c2c(ncn1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3…`
NOS RCSB PDB	1PR0	P0ABP9	268.2 Da LogP -2.27 TPSA 133.5	✓ Ro5	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO)O)O)N=…`
RAB RCSB PDB	1PW7	P0ABP9	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@H]([C@@H]([C@H](O3)C…`
TAL RCSB PDB	1OUM	P0ABP8	280.3 Da LogP -0.87 TPSA 113.5	✓ Ro5	✓ Clean	`Cc1c2c(ncn1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
TBN RCSB PDB	1PR5	P0ABP9	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`c1cn(c2c1c(ncn2)N)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
UA2 RCSB PDB	2I4T	A2E7Y6	265.3 Da LogP -1.73 TPSA 140.3	1 viol.	✓ Clean	`c1c(c2c([nH]1)c(ncn2)N)[C@H]3[C@@H]([C@@H]([C@H…`
XYA RCSB PDB	1PR6	P0ABP9	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@H]([C@H](O3)C…`

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
ZINC12503875 ZINC	1.000	250.3 Da LogP -0.22 TPSA 93.3	✓ Ro5	✓ Clean	`Cc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@@H](CO)O1`
ZINC12503877 ZINC	1.000	250.3 Da LogP -0.22 TPSA 93.3	✓ Ro5	✓ Clean	`Cc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@@H](CO)O1`
ZINC1319200 ZINC	1.000	298.3 Da LogP -0.84 TPSA 113.5	✓ Ro5	✓ Clean	`CSc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC1530555 ZINC	1.000	225.2 Da LogP -1.33 TPSA 119.0	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2COCCO)c(=O)[nH]1`
ZINC19939879 ZINC	1.000	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H…`
ZINC2047403 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H]1O`
ZINC2047404 ZINC	1.000	250.3 Da LogP -0.22 TPSA 93.3	✓ Ro5	✓ Clean	`Cc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@H](CO)O1`
ZINC2047673 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@@H]1O`
ZINC21982895 ZINC	1.000	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@H]1O[C@H](CO)[C@H](O)[C@@H]…`
ZINC22059332 ZINC	1.000	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]…`
ZINC2504595 ZINC	1.000	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@H]…`
ZINC2524720 ZINC	1.000	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@H…`
ZINC2573068 ZINC	1.000	268.2 Da LogP -2.27 TPSA 133.5	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@…`
ZINC26735509 ZINC	1.000	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H]1O`
ZINC3201876 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC3201878 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC3830178 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3830179 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3832269 ZINC	1.000	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC3872575 ZINC	1.000	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@H…`
ZINC3872576 ZINC	1.000	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@…`
ZINC3872577 ZINC	1.000	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@…`
ZINC3873955 ZINC	1.000	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3873956 ZINC	1.000	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3873957 ZINC	1.000	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H]1O`
ZINC3873958 ZINC	1.000	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC3978047 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC3978048 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC3978049 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC4015531 ZINC	1.000	268.2 Da LogP -2.27 TPSA 133.5	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C…`
ZINC4216238 ZINC	1.000	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@…`
ZINC4556963 ZINC	1.000	298.3 Da LogP -0.84 TPSA 113.5	✓ Ro5	✓ Clean	`CSc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC4556964 ZINC	1.000	298.3 Da LogP -0.84 TPSA 113.5	✓ Ro5	✓ Clean	`CSc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]…`
ZINC4556965 ZINC	1.000	298.3 Da LogP -0.84 TPSA 113.5	✓ Ro5	✓ Clean	`CSc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H…`
ZINC5127789 ZINC	1.000	268.2 Da LogP -2.27 TPSA 133.5	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@H…`
ZINC5161656 ZINC	1.000	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC5162989 ZINC	1.000	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC519129 ZINC	1.000	298.3 Da LogP -0.84 TPSA 113.5	✓ Ro5	✓ Clean	`CSc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC6019830 ZINC	1.000	298.3 Da LogP -0.84 TPSA 113.5	✓ Ro5	✓ Clean	`CSc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC6019832 ZINC	1.000	298.3 Da LogP -0.84 TPSA 113.5	✓ Ro5	✓ Clean	`CSc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H]1O`
ZINC6069212 ZINC	1.000	250.3 Da LogP -0.22 TPSA 93.3	✓ Ro5	✓ Clean	`Cc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@@H](CO)O1`
ZINC6585598 ZINC	1.000	269.2 Da LogP -0.81 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@H]1C[C@H](O)[C@@H](CO)O1`
ZINC8580514 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H]1O`
ZINC8613161 ZINC	1.000	268.2 Da LogP -2.27 TPSA 133.5	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H…`
ZINC8614390 ZINC	1.000	268.2 Da LogP -2.27 TPSA 133.5	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C…`
ZINC8652273 ZINC	1.000	268.2 Da LogP -2.27 TPSA 133.5	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@…`
ZINC8855117 ZINC	1.000	268.2 Da LogP -2.27 TPSA 133.5	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@…`
ZINC895113 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@@H]1O`
ZINC896706 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC970363 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`

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 A0A0H3GM89

Pathways

KEGG R02297 BioCyc XANTHOSINEPHOSPHORY-RXN KEGG R01863 BioCyc INOPHOSPHOR-RXN KEGG R02557 BioCyc DEOXYADENPHOSPHOR-RXN KEGG R01969 BioCyc DEOXYGUANPHOSPHOR-RXN KEGG R02748 BioCyc DEOXYINOPHOSPHOR-RXN KEGG R02147 BioCyc RXN0-5199 KEGG R01561 BioCyc ADENPHOSPHOR-RXN KEGG R09668 BioCyc RXN-12241