Protein profile

KP13_31497

Orotate phosphoribosyltransferase

Genome: KpKP13

Gene: pyrE AHE42096.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GXD7

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Amino acids 213

Annotations 8

Features 14

PDB binders 20

Druggability 0.116

Overview

Basic information about this protein and its source genome.

Accession: KP13_31497
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: pyrE AHE42096.1
Status: annotated
Amino acids: 213
Structure source: AlphaFold + ColabFold

2.4.2.10

GO:0004588 Catalysis of the reaction: orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. GO:0006221 The chemical reactions and pathways resulting in the formation of a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0000287 Binding to a magnesium (Mg) ion. GO:0006207 The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors. GO:0044205 The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD+ or oxygen.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 31.183
Human E-value: 3.16e-08
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 70.423
DEG E-value: 4.0700000000000003e-107
Localization: Cytoplasmic
ColabFold pLDDT: 95.77

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 0.116

Structure A0A0H3GXD7

Pocket Pocket 11

P2Rank 0.075

Structure A0A0H3GXD7

Pocket Pocket 1

ColabFold model

FPocket 0.034 · Pocket 7

P2Rank 0.069 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 306 / 4744 genomes with a hit

Normalized 0.065

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

2.4.2.10

Gene Ontology (GO)

GO:0004588 Catalysis of the reaction: orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate.
GO:0006221 The chemical reactions and pathways resulting in the formation of a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0006207 The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors.
GO:0044205 The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD+ or oxygen.
GO:0046132 The chemical reactions and pathways resulting in the formation of any ribonucleoside, a nucleoside in which a pyrimidine base is linked to a ribose (beta-D-ribofuranose) molecule.

Sequence Features

Domain/signature hits from InterPro and related databases.

14 records

Show feature table

Start	End	DB	Term	Name
10	187	NCBIfam	TIGR00336	orotate phosphoribosyltransferase
10	187	InterPro	IPR004467	Orotate phosphoribosyl transferase domain
1	213	PANTHER	PTHR46683	OROTATE PHOSPHORIBOSYLTRANSFERASE 1-RELATED
2	211	SUPERFAMILY	SSF53271	PRTase-like
2	211	InterPro	IPR029057	Phosphoribosyltransferase-like
1	213	Gene3D	G3DSA:3.40.50.2020	-
1	213	InterPro	IPR029057	Phosphoribosyltransferase-like
50	159	Pfam	PF00156	Phosphoribosyl transferase domain
50	159	InterPro	IPR000836	Phosphoribosyltransferase domain
1	213	Hamap	MF_01208	Orotate phosphoribosyltransferase [pyrE].
1	213	InterPro	IPR023031	Orotate phosphoribosyltransferase
1	213	FunFam	G3DSA:3.40.50.2020:FF:000008	Orotate phosphoribosyltransferase
49	174	CDD	cd06223	PRTases_typeI
49	174	InterPro	IPR000836	Phosphoribosyltransferase domain

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_A0A0H3GXD7	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_31497	ColabFold	—	—	full sequence	—	Loaded

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

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				1.5	0.022
2				1.28	0.013

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				1.5	0.021
2				1.13	0.008

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.

74 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
5BU	2QCG	P11172	403.1 Da LogP -1.97 TPSA 171.3	✓ Ro5	✓ Clean	`C1=C(C(=O)NC(=O)N1[C@H]2[C@@H]([C@@H]([C@H](O2)…`
5FU	2QCF	P11172	342.2 Da LogP -2.60 TPSA 171.3	✓ Ro5	✓ Clean	`C1=C(C(=O)NC(=O)N1[C@H]2[C@@H]([C@@H]([C@H](O2)…`
5IU	2QCH	P11172	434.1 Da LogP -1.10 TPSA 151.1	✓ Ro5	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C=C(C(=O)NC2=O)I)COP(=O…`
6AU	3L0K	P11172	366.2 Da LogP -2.53 TPSA 188.4	✓ Ro5	✓ Clean	`CC(=O)C1=CC(=O)NC(=O)N1[C@H]2[C@@H]([C@@H]([C@H…`
6CN	3EX1	P11172	349.2 Da LogP -2.86 TPSA 195.1	✓ Ro5	✓ Clean	`C1=C(N(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)O)O)O)C#N`
6ZJ	5HKI	P9WHK9	434.0 Da LogP -2.96 TPSA 198.3	1 viol.	✓ Clean	`C1C(=O)O[Fe]234(OC(=O)CC1(C(=O)O2)O)OC(=O)CC(CC…`
BMP	3BGG	P11172	340.2 Da LogP -3.03 TPSA 191.5	1 viol.	✓ Clean	`C1=C(N(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…`
CNU	3BK0	P11172	349.2 Da LogP -2.86 TPSA 195.1	✓ Ro5	✓ Clean	`C1=C(C(=O)NC(=O)N1C2C(C(C(O2)COP(=O)(O)O)O)O)C#N`
JW5	2QCM	P11172	354.2 Da LogP -3.24 TPSA 191.5	1 viol.	✓ Clean	`C1=C(N(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…`
NUP	3DBP	P11172	339.2 Da LogP -3.15 TPSA 197.3	1 viol.	✓ Clean	`C1=C(N(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…`
OMP	1STO	P08870	368.2 Da LogP -3.04 TPSA 208.6	1 viol.	✓ Clean	`C1=C(N(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…`
PFU	3MI2	P11172	339.2 Da LogP -2.51 TPSA 208.4	1 viol.	✓ Clean	`C([C@@H]1[C@H]([C@H]([C@@H](O1)c2c(c([nH]n2)C(=…`
QRT	6ZX2	P11172	367.2 Da LogP -3.64 TPSA 214.4	1 viol.	✓ Clean	`C1=C(N(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…`
QRZ	6ZX3	P11172	383.3 Da LogP -3.10 TPSA 197.3	1 viol.	✓ Clean	`C1=C(N(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…`
S5P	3L0N	P11172	356.2 Da LogP -2.45 TPSA 171.3	1 viol.	✓ Clean	`C1=C(N(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…`
U	6YVK	P11172	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
U1P	3EWW	P11172	351.2 Da LogP -2.74 TPSA 195.2	1 viol.	✓ Clean	`[H]/N=C/C1=CC(=O)NC(=O)N1[C@H]2[C@@H]([C@@H]([C…`
UEP	3EWU	P11172	352.2 Da LogP -2.17 TPSA 171.3	✓ Ro5	✓ Clean	`CCC1=CC(=O)NC(=O)N1[C@H]2[C@@H]([C@@H]([C@H](O2…`
UFT	3MO7	P11172	326.2 Da LogP -1.76 TPSA 151.1	✓ Ro5	✓ Clean	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
XMP	3BVJ	P11172	365.2 Da LogP -3.44 TPSA 201.2	1 viol.	✓ Clean	`c1[nH+]c2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=…`

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
CHEMBL2105330	P11172	7.77	259.2 Da LogP -2.63 TPSA 161.9	1 viol.	✓ Clean	`NC(=O)c1[nH]nc([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2…`
CHEMBL473587	P11172	6.46	370.2 Da LogP -2.03 TPSA 171.3	✓ Ro5	✓ Clean	`CCc1c(F)c(=O)[nH]c(=O)n1[C@@H]1O[C@H](COP(=O)(O…`
CHEMBL1164954	P11172	—	477.4 Da LogP 2.74 TPSA 91.8	✓ Ro5	✓ Clean	`CC1(C)O[C@@H]2[C@H](O1)[C@@H](CO[Si](C)(C)C(C)(…`
CHEMBL515914	P11172	—	371.3 Da LogP -1.74 TPSA 155.9	1 viol.	✓ Clean	`CC(=O)OC[C@H]1O[C@@H](n2ncc(=O)[nH]c2=O)[C@H](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
ZINC100351015	1.000	368.2 Da LogP -3.04 TPSA 208.6	1 viol.	✓ Clean	`O=C(O)c1cc(=O)[nH]c(=O)n1[C@@H]1O[C@H](COP(=O)(…`
ZINC4095542	1.000	368.2 Da LogP -3.04 TPSA 208.6	1 viol.	✓ Clean	`O=C(O)c1cc(=O)[nH]c(=O)n1[C@@H]1O[C@H](COP(=O)(…`
ZINC4217381	1.000	259.2 Da LogP -2.63 TPSA 161.9	1 viol.	✓ Clean	`NC(=O)c1[nH]nc([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2…`
ZINC5085274	1.000	259.2 Da LogP -2.63 TPSA 161.9	1 viol.	✓ Clean	`NC(=O)c1[nH]nc([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2…`
ZINC5085275	1.000	259.2 Da LogP -2.63 TPSA 161.9	1 viol.	✓ Clean	`NC(=O)c1[nH]nc([C@@H]2O[C@@H](CO)[C@H](O)[C@@H]…`
ZINC5085276	1.000	259.2 Da LogP -2.63 TPSA 161.9	1 viol.	✓ Clean	`NC(=O)c1[nH]nc([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]…`
ZINC5085278	1.000	259.2 Da LogP -2.63 TPSA 161.9	1 viol.	✓ Clean	`NC(=O)c1[nH]nc([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H…`
ZINC13547843	0.708	354.1 Da LogP -1.22 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@H]2C[C@@H](O)[C@@H](CO)O2)cc1I`
ZINC17779640	0.708	354.1 Da LogP -1.22 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@H]2C[C@H](O)[C@H](CO)O2)cc1I`
ZINC2562618	0.708	354.1 Da LogP -1.22 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@H]2C[C@@H](O)[C@H](CO)O2)cc1I`
ZINC27654519	0.708	354.1 Da LogP -1.22 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2C[C@@H](O)[C@@H](CO)O2)cc…`
ZINC3586101	0.708	354.1 Da LogP -1.22 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2C[C@H](O)[C@H](CO)O2)cc1I`
ZINC3834173	0.708	354.1 Da LogP -1.22 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@H]2C[C@H](O)[C@@H](CO)O2)cc1I`
ZINC5223557	0.708	354.1 Da LogP -1.22 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2C[C@H](O)[C@@H](CO)O2)cc1I`
ZINC537850	0.708	354.1 Da LogP -1.22 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2C[C@@H](O)[C@H](CO)O2)cc1I`
ZINC14618595	0.700	288.2 Da LogP -3.15 TPSA 162.1	✓ Ro5	✓ Clean	`O=C(O)c1cc(=O)[nH]c(=O)n1[C@@H]1O[C@H](CO)[C@@H…`
ZINC6090924	0.700	288.2 Da LogP -3.15 TPSA 162.1	✓ Ro5	✓ Clean	`O=C(O)c1cc(=O)[nH]c(=O)n1[C@@H]1O[C@H](CO)[C@@H…`
ZINC88462830	0.700	288.2 Da LogP -3.15 TPSA 162.1	✓ Ro5	✓ Clean	`O=C(O)c1cc(=O)[nH]c(=O)n1[C@@H]1O[C@H](CO)[C@H]…`
ZINC88462832	0.700	288.2 Da LogP -3.15 TPSA 162.1	✓ Ro5	✓ Clean	`O=C(O)c1cc(=O)[nH]c(=O)n1[C@@H]1O[C@H](CO)[C@H]…`
ZINC256689713	0.685	368.2 Da LogP -2.62 TPSA 208.9	1 viol.	✓ Clean	`O=C(O)c1cc(O)nc(=O)n1[C@@H]1O[C@H](COP(=O)(O)O)…`
ZINC256689719	0.685	368.2 Da LogP -2.62 TPSA 208.9	1 viol.	✓ Clean	`O=C(O)c1cc(O)nc(=O)n1[C@@H]1O[C@H](COP(=O)(O)O)…`
ZINC5385816	0.680	385.3 Da LogP -1.36 TPSA 155.9	1 viol.	✓ Clean	`CC(=O)O[C@H]1[C@@H](OC(C)=O)[C@@H](C)O[C@@H](n2…`
ZINC5385817	0.680	385.3 Da LogP -1.36 TPSA 155.9	1 viol.	✓ Clean	`CC(=O)O[C@H]1[C@H](C)O[C@@H](n2ncc(=O)[nH]c2=O)…`
ZINC5385819	0.680	385.3 Da LogP -1.36 TPSA 155.9	1 viol.	✓ Clean	`CC(=O)O[C@@H]1[C@H](OC(C)=O)[C@H](n2ncc(=O)[nH]…`
ZINC5385820	0.680	385.3 Da LogP -1.36 TPSA 155.9	1 viol.	✓ Clean	`CC(=O)O[C@@H]1[C@H](OC(C)=O)[C@H](n2ncc(=O)[nH]…`
ZINC504796802	0.667	443.4 Da LogP -1.40 TPSA 182.4	1 viol.	✓ Clean	`CC(=O)OC[C@@H]1O[C@H](n2ncc(O)nc2=O)[C@H](OC(C)…`
ZINC504796803	0.667	443.4 Da LogP -1.40 TPSA 182.4	1 viol.	✓ Clean	`CC(=O)OC[C@@H]1O[C@H](n2ncc(O)nc2=O)[C@H](OC(C)…`
ZINC504796804	0.667	443.4 Da LogP -1.40 TPSA 182.4	1 viol.	✓ Clean	`CC(=O)OC[C@@H]1O[C@H](n2ncc(O)nc2=O)[C@H](OC(C)…`
ZINC504796805	0.667	443.4 Da LogP -1.40 TPSA 182.4	1 viol.	✓ Clean	`CC(=O)OC[C@@H]1O[C@H](n2ncc(O)nc2=O)[C@H](OC(C)…`
ZINC8740070	0.667	412.4 Da LogP -1.08 TPSA 165.0	1 viol.	✓ Clean	`CC(=O)Nc1cnn([C@@H]2O[C@H](COC(C)=O)[C@@H](OC(C…`
ZINC102809055	0.632	486.4 Da LogP -1.75 TPSA 185.4	1 viol.	✓ Clean	`CC(=O)OC[C@@H]1O[C@H](n2nc(N(C)C)c(=O)[nH]c2=O)…`
ZINC102809059	0.632	486.4 Da LogP -1.75 TPSA 185.4	1 viol.	✓ Clean	`CC(=O)OC[C@H]1O[C@@H](n2nc(N(C)C)c(=O)[nH]c2=O)…`
ZINC34716119	0.632	486.4 Da LogP -1.75 TPSA 185.4	1 viol.	✓ Clean	`CC(=O)OC[C@@H]1O[C@@H](n2nc(N(C)C)c(=O)[nH]c2=O…`
ZINC34716121	0.632	486.4 Da LogP -1.75 TPSA 185.4	1 viol.	✓ Clean	`CC(=O)OC[C@H]1O[C@@H](n2nc(N(C)C)c(=O)[nH]c2=O)…`
ZINC34716123	0.632	486.4 Da LogP -1.75 TPSA 185.4	1 viol.	✓ Clean	`CC(=O)OC[C@@H]1O[C@@H](n2nc(N(C)C)c(=O)[nH]c2=O…`
ZINC9033302	0.632	486.4 Da LogP -1.75 TPSA 185.4	1 viol.	✓ Clean	`CC(=O)OC[C@H]1O[C@@H](n2nc(N(C)C)c(=O)[nH]c2=O)…`
ZINC12659241	0.621	427.4 Da LogP -0.47 TPSA 145.0	1 viol.	✓ Clean	`CCCCn1c(=O)cnn([C@@H]2O[C@H](COC(C)=O)[C@@H](OC…`
ZINC12659244	0.621	427.4 Da LogP -0.47 TPSA 145.0	1 viol.	✓ Clean	`CCCCn1c(=O)cnn([C@@H]2O[C@H](COC(C)=O)[C@H](OC(…`
ZINC12659247	0.621	427.4 Da LogP -0.47 TPSA 145.0	1 viol.	✓ Clean	`CCCCn1c(=O)cnn([C@@H]2O[C@H](COC(C)=O)[C@H](OC(…`
ZINC8770561	0.621	427.4 Da LogP -0.47 TPSA 145.0	1 viol.	✓ Clean	`CCCCn1c(=O)cnn([C@@H]2O[C@H](COC(C)=O)[C@@H](OC…`
ZINC12503831	0.611	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]2…`
ZINC12503833	0.611	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H]…`
ZINC13512000	0.611	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC1532538	0.611	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC2026984	0.611	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC2606131	0.611	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC36377965	0.611	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC3870257	0.611	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC3870260	0.611	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC9235501	0.611	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@H](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.