Protein profile

KP13_02013

Purine nucleoside phosphorylase deoD-type

Genome: KpKP13

Gene: deoD AHE46450.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GM89

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Amino acids 239

Annotations 9

Features 16

PDB binders 26

Druggability 0.684

Overview

Basic information about this protein and its source genome.

Accession: KP13_02013
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: deoD AHE46450.1
Status: annotated
Amino acids: 239
Structure source: AlphaFold + ColabFold

2.4.2.1

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: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:0006139 Any cellular metabolic process involving nucleobases, nucleosides, nucleotides and nucleic acids. GO:0016763 Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor). GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 44.589
DEG E-value: 7.28e-61
Localization: Cytoplasmic
ColabFold pLDDT: 97.12

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.684

Structure A0A0H3GM89

Pocket Pocket 6

P2Rank 0.797

Structure A0A0H3GM89

Pocket Pocket 1

ColabFold model

FPocket 0.899 · Pocket 1

P2Rank 0.795 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 877 / 4744 genomes with a hit

Normalized 0.185

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

2.4.2.1

Gene Ontology (GO)

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: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:0006139 Any cellular metabolic process involving nucleobases, nucleosides, nucleotides and nucleic acids.
GO:0016763 Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor).
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 Features

Domain/signature hits from InterPro and related databases.

16 records

Show feature table

Start	End	DB	Term	Name
5	234	NCBIfam	TIGR00107	purine-nucleoside phosphorylase
5	234	InterPro	IPR004402	Purine nucleoside phosphorylase DeoD-type
5	232	CDD	cd09006	PNP_EcPNPI-like
5	232	InterPro	IPR004402	Purine nucleoside phosphorylase DeoD-type
62	77	ProSitePatterns	PS01232	Purine and other phosphorylases family 1 signature.
62	77	InterPro	IPR018016	Nucleoside phosphorylase, conserved site
15	220	Pfam	PF01048	Phosphorylase superfamily
15	220	InterPro	IPR000845	Nucleoside phosphorylase domain
3	234	SUPERFAMILY	SSF53167	Purine and uridine phosphorylases
3	234	InterPro	IPR035994	Nucleoside phosphorylase superfamily
2	235	Hamap	MF_01627	Purine nucleoside phosphorylase DeoD-type [deoD].
2	235	InterPro	IPR004402	Purine nucleoside phosphorylase DeoD-type
1	238	Gene3D	G3DSA:3.40.50.1580	Nucleoside phosphorylase domain
1	238	InterPro	IPR035994	Nucleoside phosphorylase superfamily
1	235	FunFam	G3DSA:3.40.50.1580:FF:000002	Purine nucleoside phosphorylase DeoD-type
4	232	PANTHER	PTHR43691	URIDINE PHOSPHORYLASE

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GM89	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_02013	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
6				0.684

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				9.22	0.494
2				5.6	0.269

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
1				0.899

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				7.45	0.391
2				6.25	0.313

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

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	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	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	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	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	1OTY	P0ABP8	134.1 Da LogP 0.66 TPSA 54.5	✓ Ro5	✓ Clean	`Cc1c2c(nc[nH]2)ncn1`
7HX	5IU6	P0ABP8	135.1 Da LogP 0.66 TPSA 61.8	✓ Ro5	✓ Clean	`c1c[nH]c2c1c(ncn2)O`
AC2	5I3C	A7ZVS7	225.2 Da LogP -1.33 TPSA 119.0	✓ Ro5	✓ Clean	`c1nc2c(n1COCCO)N=C(NC2=O)N`
ADE	4D8V	O34925	135.1 Da LogP -0.06 TPSA 80.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)c(ncn2)N`
ADN	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	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	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	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	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	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	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	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	4DA6	O34925	255.2 Da LogP -1.97 TPSA 139.3	✓ Ro5	✓ Clean	`c1nc2c(n1COC(CO)CO)N=C(NC2=O)N`
HPA	5MX6	P56463	136.1 Da LogP -0.35 TPSA 74.4	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)N=CNC2=O`
MDR	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	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	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	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	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	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	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	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	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	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	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	1.000	225.2 Da LogP -1.33 TPSA 119.0	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2COCCO)c(=O)[nH]1`
ZINC19939879	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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.