Protein profile

KP13_22167

Ribonucleoside-diphosphate reductase 2 subunit alpha

Genome: KpKP13

Gene: ANJ86589.1 nrdE Structure source: AlphaFold + ColabFold UniProt A0A0H3GWI4

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Amino acids 713

Annotations 6

Features 32

PDB binders 14

Druggability 0.238

Overview

Basic information about this protein and its source genome.

Accession: KP13_22167
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: ANJ86589.1 nrdE
Status: annotated
Amino acids: 713
Structure source: AlphaFold + ColabFold

1.17.4.1

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA. GO:0004748 Catalysis of the reaction: 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin. Thioredoxin disulfide is the oxidized form of thioredoxin. GO:0005971 An enzyme complex composed of 2-4 or more subunits, which usually contains nonheme iron and requires ATP for catalysis. Catalyzes the formation of 2'-deoxyribonucleoside diphosphate from ribonucleoside diphosphate, using either thioredoxin disulfide or glutaredoxin disulfide as an acceptor. GO:0009263 The chemical reactions and pathways resulting in the formation of a deoxyribonucleotide, a compound consisting of deoxyribonucleoside (a base linked to a deoxyribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 33.962
Human E-value: 1.28e-10
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 71.031
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 93.58

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 0.238

Structure A0A0H3GWI4

Pocket Pocket 45

P2Rank 0.777

Structure A0A0H3GWI4

Pocket Pocket 1

ColabFold model

FPocket 0.55 · Pocket 26

P2Rank 0.757 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 228 / 4744 genomes with a hit

Normalized 0.048

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1.17.4.1

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
GO:0004748 Catalysis of the reaction: 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin. Thioredoxin disulfide is the oxidized form of thioredoxin.
GO:0005971 An enzyme complex composed of 2-4 or more subunits, which usually contains nonheme iron and requires ATP for catalysis. Catalyzes the formation of 2'-deoxyribonucleoside diphosphate from ribonucleoside diphosphate, using either thioredoxin disulfide or glutaredoxin disulfide as an acceptor.
GO:0009263 The chemical reactions and pathways resulting in the formation of a deoxyribonucleotide, a compound consisting of deoxyribonucleoside (a base linked to a deoxyribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.

Sequence Features

Domain/signature hits from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
127	694	CDD	cd01679	RNR_I
176	693	Pfam	PF02867	Ribonucleotide reductase, barrel domain
176	693	InterPro	IPR000788	Ribonucleotide reductase large subunit, C-terminal
98	170	Pfam	PF00317	Ribonucleotide reductase, all-alpha domain
98	170	InterPro	IPR013509	Ribonucleotide reductase large subunit, N-terminal
14	173	SUPERFAMILY	SSF48168	R1 subunit of ribonucleotide reductase, N-terminal domain
14	173	InterPro	IPR008926	Ribonucleotide reductase R1 subunit, N-terminal
174	697	SUPERFAMILY	SSF51998	PFL-like glycyl radical enzymes
159	694	Gene3D	G3DSA:3.20.70.20	-
94	699	PANTHER	PTHR11573	RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN
94	699	InterPro	IPR039718	Ribonucleoside-diphosphate reductase large subunit
565	587	ProSitePatterns	PS00089	Ribonucleotide reductase large subunit signature.
565	587	InterPro	IPR013346	Ribonucleotide reductase, class I, alpha subunit, C-terminal
294	346	Gene3D	G3DSA:1.10.1650.20	-
102	695	NCBIfam	TIGR02506	ribonucleoside-diphosphate reductase subunit alpha
102	695	InterPro	IPR013346	Ribonucleotide reductase, class I, alpha subunit, C-terminal
15	96	Pfam	PF08343	Ribonucleotide reductase N-terminal
15	96	InterPro	IPR013554	Ribonucleotide reductase N-terminal
464	486	PRINTS	PR01183	Ribonucleotide reductase large chain signature
464	486	InterPro	IPR000788	Ribonucleotide reductase large subunit, C-terminal
576	603	PRINTS	PR01183	Ribonucleotide reductase large chain signature
576	603	InterPro	IPR000788	Ribonucleotide reductase large subunit, C-terminal
381	392	PRINTS	PR01183	Ribonucleotide reductase large chain signature
381	392	InterPro	IPR000788	Ribonucleotide reductase large subunit, C-terminal
425	448	PRINTS	PR01183	Ribonucleotide reductase large chain signature
425	448	InterPro	IPR000788	Ribonucleotide reductase large subunit, C-terminal
492	515	PRINTS	PR01183	Ribonucleotide reductase large chain signature
492	515	InterPro	IPR000788	Ribonucleotide reductase large subunit, C-terminal
250	269	PRINTS	PR01183	Ribonucleotide reductase large chain signature
250	269	InterPro	IPR000788	Ribonucleotide reductase large subunit, C-terminal
14	713	NCBIfam	TIGR04170	class 1b ribonucleoside-diphosphate reductase subunit alpha
14	713	InterPro	IPR026459	Ribonucleotide reductase, class 1b, subunit NrdE

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_A0A0H3GWI4	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_22167	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
45				0.238

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	10.11	0.544
2	3.53	0.13
3	3.21	0.11
4	2.86	0.09
5	1.62	0.026

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
26				0.55
6				0.328

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	9.22	0.494
2	5.47	0.26
3	3.74	0.143
4	2.13	0.049
5	1.82	0.035

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.

73 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
2A5	3K8T	P21524	455.3 Da LogP -1.11 TPSA 232.6	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
3X4	4X3V	P23921	418.5 Da LogP -0.12 TPSA 158.9	✓ Ro5	✓ Clean	`CC(C)(C(=O)NCCCC[C@H](C(=O)O)N)NC(=O)CN1C(=O)c2…`
7LL	5TUS	P23921	306.3 Da LogP 3.01 TPSA 81.9	✓ Ro5	Alert	`c1ccc2c(c1)ccc(c2/C=N\NC(=O)c3ccccc3O)O`
ANP	2CVT	P21524	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
DCP	1PEO	Q08698	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C=CC(=NC2=O)N)CO[P@@](=…`
DGT	2BQ1	Q08698	507.2 Da LogP -1.31 TPSA 278.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3C[C@@H]([C@H](O3)CO[P@@](=O)(O)O…`
DTP	1PEU	Q08698	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3C[C@@H]([C@H](O3)CO[P@]…`
E4X	6L3R	P23921	488.4 Da LogP 4.10 TPSA 105.1	✓ Ro5	✓ Clean	`C[C@H](c1cccc2c1cccc2)[C@@H](C3=NNC(=O)O3)NS(=O…`
E6O	6L7L	P23921	476.9 Da LogP 2.43 TPSA 148.2	✓ Ro5	✓ Clean	`C[C@H](c1cccc2c1CCC2)[C@@H](C3=NNC(=O)O3)NS(=O)…`
EJ6	6LKM	P23921	511.0 Da LogP 3.42 TPSA 117.5	1 viol.	✓ Clean	`Cc1ccc(c(c1C)[C@@H](C)[C@@H](C2=NNC(=O)O2)NS(=O…`
GCQ	2EUD	P21524	423.2 Da LogP -1.05 TPSA 203.7	✓ Ro5	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2C([C@@H]([C@H](O2)CO[P@]…`
MRT	2ZLG	P21524	1031.2 Da LogP 4.98 TPSA 286.9	3 viol.	✓ Clean	`CC(C)C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](…`
N5P	3RSR	P21524	518.2 Da LogP 1.54 TPSA 237.3	2 viol.	✓ Clean	`c1cc2c(ccn2C3CC(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(…`
TTP	6MT9	P50620	482.2 Da LogP -1.16 TPSA 244.1	2 viol.	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO[P@]…`

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
CHEMBL3235141	P23921	—	342.3 Da LogP 0.10 TPSA 115.5	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CNCc3ccco3)[C@@H](O)C2(F)F…`
CHEMBL3235142	P23921	—	373.4 Da LogP -1.07 TPSA 122.7	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CNCCN3CCCC3=O)[C@@H](O)C2(…`
CHEMBL3235143	P23921	—	370.4 Da LogP -0.20 TPSA 120.2	✓ Ro5	✓ Clean	`C[C@H](NC[C@H]1O[C@@H](n2ccc(N)nc2=O)C(F)(F)[C@…`
CHEMBL3235144	P23921	—	368.3 Da LogP -0.57 TPSA 111.4	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CN3CCn4nccc4C3)[C@@H](O)C2…`
CHEMBL4059739	P23921	—	399.2 Da LogP 4.08 TPSA 70.9	✓ Ro5	Alert	`COc1cc(Br)ccc1C(=O)N/N=C/c1c(O)ccc2ccccc12`
CHEMBL4067105	P23921	—	306.3 Da LogP 3.01 TPSA 81.9	✓ Ro5	Alert	`O=C(N/N=C/c1c(O)ccc2ccccc12)c1ccccc1O`
CHEMBL4073197	P23921	—	339.8 Da LogP 3.54 TPSA 87.7	✓ Ro5	Alert	`Nc1ccc(C(=O)N/N=C/c2c(O)ccc3ccccc23)cc1Cl`
CHEMBL4100050	P23921	—	306.3 Da LogP 3.01 TPSA 81.9	✓ Ro5	✓ Clean	`O=C(N/N=C/c1ccc2cc(O)ccc2c1)c1ccccc1O`
GEO	P23921	—	263.2 Da LogP -1.29 TPSA 110.6	✓ Ro5	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2C([C@@H]([C@H](O2)CO)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
ZINC13434879	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@H](CO[P@@](=O)…`
ZINC13434881	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@H](CO[P@@](=O)(…`
ZINC13434883	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@H](CO[P@@](=O…`
ZINC13434884	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@H](CO[P@@](=O)…`
ZINC33979251	1.000	482.2 Da LogP -1.16 TPSA 244.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC8215662	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@@H](CO[P@@](=O)…`
ZINC8664605	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@@H](CO[P@@](=O…`
ZINC12495199	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@@H](CO[P@@](=O…`
ZINC13434873	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@H](CO[P@@](=O)…`
ZINC13434875	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@H](CO[P@@](=O)(…`
ZINC13434876	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@H](CO[P@](=O)…`
ZINC13434878	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@H](CO[P@@](=O)…`
ZINC8215728	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@@H](CO[P@@](=O)…`
ZINC196576711	0.842	490.2 Da LogP -0.63 TPSA 264.7	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](N)[C@H](CO[P@@](=O)…`
ZINC12958401	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@@H](COP(=O)(O)…`
ZINC13538980	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@@H](COP(=O)(O…`
ZINC13538982	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@@H](COP(=O)(O)…`
ZINC1532626	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@H](COP(=O)(O)…`
ZINC1713574	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@@H](COP(=O)(O)O…`
ZINC3869813	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@H](COP(=O)(O)O…`
ZINC3869814	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@H](COP(=O)(O)O)…`
ZINC3869815	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@H](COP(=O)(O)O…`
ZINC8217141	0.807	492.2 Da LogP -0.48 TPSA 253.1	2 viol.	✓ Clean	`O=P(O)(O)O[P@](=O)(O)O[P@](=O)(O)OC[C@H]1O[C@@H…`
ZINC12501218	0.733	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC12501706	0.733	475.2 Da LogP 0.43 TPSA 238.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1CC[C@@H](CO[P@](=O)(O)O[P@@…`
ZINC12501708	0.733	475.2 Da LogP 0.43 TPSA 238.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1CC[C@H](CO[P@@](=O)(O)O[P@…`
ZINC13540909	0.733	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC12360002	0.729	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703	0.729	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599	0.729	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165	0.729	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053	0.729	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433	0.729	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898	0.729	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.729	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020	0.729	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.729	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022	0.729	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC138163261	0.721	490.2 Da LogP 0.01 TPSA 246.0	2 viol.	✓ Clean	`Nc1ncnc2c1ccn2[C@@H]1C[C@H](O)[C@H](CO[P@@](=O)…`
ZINC62613203	0.721	492.2 Da LogP -0.89 TPSA 252.8	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1C[C@H](O)[C@H](CO[P@@]…`
ZINC62613207	0.721	492.2 Da LogP -0.89 TPSA 252.8	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1C[C@H](O)[C@H](CO[P@@](…`
ZINC62613214	0.721	492.2 Da LogP -0.89 TPSA 252.8	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1C[C@@H](O)[C@H](CO[P@@]…`
ZINC72370084	0.675	397.4 Da LogP 3.89 TPSA 113.1	✓ Ro5	Alert	`N=C(N/N=C/c1c(O)ccc2ccccc12)N/N=C/c1c(O)ccc2ccc…`
ZINC12503703	0.672	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@H](O)[C@@H](CO[P@@](=O)(…`
ZINC8215878	0.672	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O…`
ZINC111485802	0.667	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncc2ncn([C@@H]3C[C@H](O)[C@H](CO[P@@](=O)(O)…`
ZINC136782209	0.667	305.2 Da LogP -0.91 TPSA 113.7	✓ Ro5	✓ Clean	`CC(=O)Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)C2(F)F)c…`
ZINC13522804	0.661	332.2 Da LogP -0.71 TPSA 160.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](n2cnc3c(O)ncnc32)C[C@@…`
ZINC17312285	0.659	414.5 Da LogP 4.24 TPSA 89.2	✓ Ro5	Alert	`Oc1ccc2ccccc2c1/C=N\NC(=S)N/N=C/c1c(O)ccc2ccccc…`
ZINC4721014	0.659	414.5 Da LogP 4.24 TPSA 89.2	✓ Ro5	Alert	`Oc1ccc2ccccc2c1/C=N\NC(=S)N/N=C\c1c(O)ccc2ccccc…`

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.