Protein profile

KP13_02015

Thymidine phosphorylase

Genome: KpKP13

Gene: AHE46452.1 deoA Structure source: AlphaFold + ColabFold UniProt A0A0H3GRD1

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Amino acids 440

Annotations 10

Features 32

PDB binders 7

Druggability 0.835

Overview

Basic information about this protein and its source genome.

Accession: KP13_02015
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE46452.1 deoA
Status: annotated
Amino acids: 440
Structure source: AlphaFold + ColabFold

2.4.2.4

GO:0006206 The chemical reactions and pathways involving pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases. GO:0009032 Catalysis of the reaction: thymidine + phosphate = thymine + 2-deoxy-D-ribose 1-phosphate. GO:0016757 Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor). GO:0004645 Catalysis of the reaction: 1,4-alpha-D-glucosyl(n) + phosphate = 1,4-alpha-D-glucosyl(n-1) + alpha-D-glucose 1-phosphate. GO:0006213 The chemical reactions and pathways involving any pyrimidine nucleoside, one of a family of organic molecules consisting of a pyrimidine base covalently bonded to ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside). GO:0016763 Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor).

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 51.852
Human E-value: 8.49e-09
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 96.24

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 0.835

Structure A0A0H3GRD1

Pocket Pocket 4

P2Rank 0.915

Structure A0A0H3GRD1

Pocket Pocket 1

ColabFold model

FPocket 0.558 · Pocket 3

P2Rank 0.869 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 155 / 4744 genomes with a hit

Normalized 0.033

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

2.4.2.4

Gene Ontology (GO)

GO:0006206 The chemical reactions and pathways involving pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
GO:0009032 Catalysis of the reaction: thymidine + phosphate = thymine + 2-deoxy-D-ribose 1-phosphate.
GO:0016757 Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
GO:0004645 Catalysis of the reaction: 1,4-alpha-D-glucosyl(n) + phosphate = 1,4-alpha-D-glucosyl(n-1) + alpha-D-glucose 1-phosphate.
GO:0006213 The chemical reactions and pathways involving any pyrimidine nucleoside, one of a family of organic molecules consisting of a pyrimidine base covalently bonded to ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
GO:0016763 Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor).
GO:0016154 Catalysis of the reaction: pyrimidine nucleoside + phosphate = pyrimidine + alpha-D-ribose 1-phosphate.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0046104 The chemical reactions and pathways involving thymidine, deoxyribosylthymine thymine 2-deoxyriboside, a deoxynucleoside very widely distributed but occurring almost entirely as phosphoric esters in deoxynucleotides and deoxyribonucleic acid, DNA.

Sequence Features

Domain/signature hits from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
350	424	SMART	SM00941	PYNP_C_2
350	424	InterPro	IPR013102	Pyrimidine nucleoside phosphorylase, C-terminal
70	335	FunFam	G3DSA:3.40.1030.10:FF:000001	Thymidine phosphorylase
74	334	SUPERFAMILY	SSF52418	Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain
74	334	InterPro	IPR035902	Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain superfamily
6	67	Pfam	PF02885	Glycosyl transferase family, helical bundle domain
6	67	InterPro	IPR017459	Glycosyl transferase family 3, N-terminal domain
5	423	NCBIfam	TIGR02644	pyrimidine-nucleoside phosphorylase
5	423	InterPro	IPR018090	Pyrimidine-nucleoside phosphorylase, bacterial/eukaryotic
337	433	Gene3D	G3DSA:3.90.1170.30	-
337	433	InterPro	IPR036566	Pyrimidine nucleoside phosphorylase-like, C-terminal domain superfamily
2	438	NCBIfam	TIGR02643	thymidine phosphorylase
2	438	InterPro	IPR013465	Thymidine phosphorylase
350	423	Pfam	PF07831	Pyrimidine nucleoside phosphorylase C-terminal domain
350	423	InterPro	IPR013102	Pyrimidine nucleoside phosphorylase, C-terminal
337	439	SUPERFAMILY	SSF54680	Pyrimidine nucleoside phosphorylase C-terminal domain
337	439	InterPro	IPR036566	Pyrimidine nucleoside phosphorylase-like, C-terminal domain superfamily
79	309	Pfam	PF00591	Glycosyl transferase family, a/b domain
79	309	InterPro	IPR000312	Glycosyl transferase, family 3
70	325	Gene3D	G3DSA:3.40.1030.10	Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain
70	325	InterPro	IPR035902	Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain superfamily
3	439	PANTHER	PTHR10515	THYMIDINE PHOSPHORYLASE
3	439	InterPro	IPR000053	Thymidine/pyrimidine-nucleoside phosphorylase
6	194	Gene3D	G3DSA:1.20.970.10	Transferase, Pyrimidine Nucleoside Phosphorylase; Chain C
337	433	FunFam	G3DSA:3.90.1170.30:FF:000001	Thymidine phosphorylase
2	70	SUPERFAMILY	SSF47648	Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain
2	70	InterPro	IPR036320	Glycosyl transferase family 3, N-terminal domain superfamily
1	439	PIRSF	PIRSF000478	TP_PyNP
1	439	InterPro	IPR000053	Thymidine/pyrimidine-nucleoside phosphorylase
113	128	ProSitePatterns	PS00647	Thymidine and pyrimidine-nucleoside phosphorylases signature.
113	128	InterPro	IPR017872	Pyrimidine-nucleoside phosphorylase, conserved site
2	438	Hamap	MF_01628	Thymidine phosphorylase [deoA].

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_A0A0H3GRD1	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_02015	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
4				0.835

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				19.98	0.848
2				4.72	0.207

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
3				0.558

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	Score	Probability
1	15.29	0.751
2	2.19	0.052
3	1.91	0.039
4	1.09	0.007

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.

71 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
0NP	4EAD	P07650	272.2 Da LogP -1.32 TPSA 134.6	✓ Ro5	Alert	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
AZZ	4LHM	P07650	267.2 Da LogP -0.20 TPSA 133.1	✓ Ro5	Alert	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO)N=[…`
CTN	5EY3	Q7CP66	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
IUR	2WK6	P19971	238.0 Da LogP -0.33 TPSA 65.7	✓ Ro5	✓ Clean	`C1=C(C(=O)NC(=O)N1)I`
THM	4YEK	Q7CP66	242.2 Da LogP -1.51 TPSA 104.6	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO)O`
URA	1BRW	P77836	112.1 Da LogP -0.94 TPSA 65.7	✓ Ro5	✓ Clean	`C1=CNC(=O)NC1=O`
URI	4YYY	Q7CP66	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL597306	Q5FVR2	7.96	319.2 Da LogP -1.64 TPSA 152.9	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2CN(C(=O)P(=O)(O)O)C[C@@H]2O)c(=O)[…`
CHEMBL609919	Q5FVR2	7.82	335.3 Da LogP -1.47 TPSA 135.9	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2CN(C(=S)P(=O)(O)O)C[C@@H]2O)c(=O)[…`
CHEMBL599543	Q5FVR2	7.35	333.2 Da LogP -1.25 TPSA 152.9	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](CO)N(C(=O)P(=O)(O)O)C2)c(=O)…`
CHEMBL599563	Q5FVR2	7.35	305.2 Da LogP -1.80 TPSA 135.9	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2CN(CP(=O)(O)O)C[C@@H]2O)c(=O)[nH]c…`
CHEMBL598328	Q5FVR2	6.72	319.3 Da LogP -0.45 TPSA 115.6	✓ Ro5	✓ Clean	`Cc1cn(C2CCN(C(=S)P(=O)(O)O)C2)c(=O)[nH]c1=O`
CHEMBL599562	Q5FVR2	6.66	319.2 Da LogP -1.64 TPSA 152.9	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2CN(C(=O)P(=O)(O)O)C[C@H]2O)c(=O)[n…`
CHEMBL374140	P19971	6.63	364.2 Da LogP -1.98 TPSA 160.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@H]3O[C@@H](CP(=O)(O)O…`
CHEMBL401998	P19971	6.63	264.2 Da LogP -1.00 TPSA 121.6	✓ Ro5	✓ Clean	`Cc1cn(CCOCP(=O)(O)O)c(=O)[nH]c1=O`
CHEMBL597717	P19971	6.63	515.3 Da LogP -0.10 TPSA 171.4	1 viol.	✓ Clean	`O=c1c(Br)cn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c…`
CHEMBL599022	P19971	6.63	294.2 Da LogP -1.64 TPSA 141.8	✓ Ro5	✓ Clean	`Cc1cn(CC(CO)OCP(=O)(O)O)c(=O)[nH]c1=O`
CHEMBL599755	P19971	6.63	278.2 Da LogP -0.61 TPSA 121.6	✓ Ro5	✓ Clean	`Cc1cn(CC(C)OCP(=O)(O)O)c(=O)[nH]c1=O`
CHEMBL599544	Q5FVR2	6.60	319.3 Da LogP -1.41 TPSA 135.9	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](CO)N(CP(=O)(O)O)C2)c(=O)[nH]…`
CHEMBL598327	Q5FVR2	6.46	303.2 Da LogP -0.61 TPSA 132.7	✓ Ro5	✓ Clean	`Cc1cn(C2CCN(C(=O)P(=O)(O)O)C2)c(=O)[nH]c1=O`
CHEMBL373989	P07650	6.00	362.3 Da LogP -1.31 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@H]3C[C@@H](CP(=O)(O)O…`

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
ZINC1078621	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)n1`
ZINC1092752	1.000	238.0 Da LogP -0.33 TPSA 65.7	✓ Ro5	✓ Clean	`O=c1[nH]cc(I)c(=O)[nH]1`
ZINC11525575	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)[n…`
ZINC11525576	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)[…`
ZINC12336757	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)n1`
ZINC12336758	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)n1`
ZINC1446448	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)[…`
ZINC16969357	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC1842580	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC2159	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC2545102	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC2565479	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O…`
ZINC25672	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC2572653	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]c1…`
ZINC2583632	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)n1`
ZINC2583633	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)…`
ZINC3795098	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)…`
ZINC3830623	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)n1`
ZINC3830624	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)…`
ZINC3831529	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC3831621	1.000	267.2 Da LogP -0.20 TPSA 133.1	✓ Ro5	Alert	`Cc1cn([C@H]2C[C@@H](N=[N+]=[N-])[C@H](CO)O2)c(=…`
ZINC3834164	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O…`
ZINC3870261	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)…`
ZINC3870262	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O…`
ZINC3870263	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c(=O…`
ZINC3870264	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c(=…`
ZINC3978018	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)n1`
ZINC5765078	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC6072455	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC6091549	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)[…`
ZINC6091575	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC6234828	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC6524831	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)…`
ZINC6524892	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC7998085	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)…`
ZINC8613151	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)…`
ZINC8613153	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)[…`
ZINC895165	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O)…`
ZINC895248	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O)n1`
ZINC4804742	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](O)[C@H](CO)O2)c(=O)…`
ZINC4804743	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](O)[C@H](CO)O2)c(=O)[…`
ZINC4804744	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](O)[C@H](CO)O2)c(=O…`
ZINC4804745	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](O)[C@H](CO)O2)c(=O)…`
ZINC34085615	0.829	242.2 Da LogP -2.60 TPSA 136.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2N)c(=O)n1`
ZINC13546396	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2F)c(=O)n1`
ZINC16928956	0.810	258.3 Da LogP -0.14 TPSA 87.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]c1=S`
ZINC2522524	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2F)c(=O)n1`
ZINC3817231	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2F)c(=O)n1`
ZINC57331	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2F)c(=O)…`
ZINC59201305	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2F)c(=O)n1`

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.