Protein profile

VK055_1830

glutamine--tRNA ligase

Genome: KpATCC43816

Gene: glnS AIK80443.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GPY5

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Amino acids 555

Annotations 12

Features 37

PDB binders 8

Druggability 0.933

Overview

Basic information about this protein and its source genome.

Accession: VK055_1830
Assembly: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene: glnS AIK80443.1
Status: annotated
Amino acids: 555
Structure source: AlphaFold + ColabFold

6.1.1.18

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0043039 The chemical reactions and pathways by which the various amino acids become bonded to their corresponding tRNAs. The most common route for synthesis of aminoacyl tRNA is by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, usually catalyzed by the cognate aminoacyl-tRNA ligase. A given aminoacyl-tRNA ligase aminoacylates all species of an isoaccepting group of tRNA molecules. GO:0004819 Catalysis of the reaction: ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln). GO:0004812 Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP. GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. GO:0006418 The synthesis of aminoacyl tRNA by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, to be used in ribosome-mediated polypeptide synthesis.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 69.697
Human E-value: 2.15e-07
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 94.955
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 95.4

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 0.933

Structure A0A0H3GPY5

Pocket Pocket 1

P2Rank 0.886

Structure A0A0H3GPY5

Pocket Pocket 1

ColabFold model

FPocket 0.231 · Pocket 2

P2Rank 0.877 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 2315 / 4744 genomes with a hit

Normalized 0.488

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 GO

Enzyme Commission (EC)

6.1.1.18

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0043039 The chemical reactions and pathways by which the various amino acids become bonded to their corresponding tRNAs. The most common route for synthesis of aminoacyl tRNA is by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, usually catalyzed by the cognate aminoacyl-tRNA ligase. A given aminoacyl-tRNA ligase aminoacylates all species of an isoaccepting group of tRNA molecules.
GO:0004819 Catalysis of the reaction: ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln).
GO:0004812 Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP.
GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
GO:0006418 The synthesis of aminoacyl tRNA by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, to be used in ribosome-mediated polypeptide synthesis.
GO:0006412 The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
GO:0006425 The process of coupling glutamine to glutaminyl-tRNA, catalyzed by glutaminyl-tRNA synthetase. The glutaminyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a glutamine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0006424 The process of coupling glutamate to glutamyl-tRNA, catalyzed by glutamyl-tRNA synthetase. The glutamyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a glutamic acid-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.

Sequence Features

Domain/signature hits from InterPro and related databases.

37 records

Show feature table

Start	End	DB	Term	Name
1	343	FunFam	G3DSA:3.40.50.620:FF:000037	Glutamine--tRNA ligase cytoplasmic
101	209	FunFam	G3DSA:3.90.800.10:FF:000001	Glutamine--tRNA ligase
336	463	FunFam	G3DSA:2.40.240.10:FF:000001	Glutamine--tRNA ligase
101	209	Gene3D	G3DSA:3.90.800.10	-
336	463	Gene3D	G3DSA:2.40.240.10	Ribosomal Protein L25; Chain P
336	463	InterPro	IPR020056	Ribosomal protein L25/Gln-tRNA synthetase, N-terminal
28	337	Pfam	PF00749	tRNA synthetases class I (E and Q), catalytic domain
28	337	InterPro	IPR020058	Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domain
464	548	FunFam	G3DSA:2.40.240.10:FF:000003	Glutamine--tRNA ligase
28	552	NCBIfam	TIGR00440	glutamine--tRNA ligase
28	552	InterPro	IPR004514	Glutamine-tRNA synthetase
464	548	Gene3D	G3DSA:2.40.240.10	Ribosomal Protein L25; Chain P
464	548	InterPro	IPR020056	Ribosomal protein L25/Gln-tRNA synthetase, N-terminal
340	529	Pfam	PF03950	tRNA synthetases class I (E and Q), anti-codon binding domain
340	529	InterPro	IPR020059	Glutamyl/glutaminyl-tRNA synthetase, class Ib, anti-codon binding domain
60	73	PRINTS	PR00987	Glutamyl-tRNA synthetase signature
60	73	InterPro	IPR000924	Glutamyl/glutaminyl-tRNA synthetase
45	56	PRINTS	PR00987	Glutamyl-tRNA synthetase signature
45	56	InterPro	IPR000924	Glutamyl/glutaminyl-tRNA synthetase
31	43	PRINTS	PR00987	Glutamyl-tRNA synthetase signature
31	43	InterPro	IPR000924	Glutamyl/glutaminyl-tRNA synthetase
210	220	PRINTS	PR00987	Glutamyl-tRNA synthetase signature
210	220	InterPro	IPR000924	Glutamyl/glutaminyl-tRNA synthetase
340	548	SUPERFAMILY	SSF50715	Ribosomal protein L25-like
340	548	InterPro	IPR011035	Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain superfamily
261	338	FunFam	G3DSA:1.10.1160.10:FF:000001	Glutamine--tRNA ligase
10	337	SUPERFAMILY	SSF52374	Nucleotidylyl transferase
27	342	CDD	cd00807	GlnRS_core
34	45	ProSitePatterns	PS00178	Aminoacyl-transfer RNA synthetases class-I signature.
34	45	InterPro	IPR001412	Aminoacyl-tRNA synthetase, class I, conserved site
261	335	Gene3D	G3DSA:1.10.1160.10	-
261	335	InterPro	IPR020061	Glutamine-tRNA ligase, alpha-bundle domain superfamily
23	549	PANTHER	PTHR43097	GLUTAMINE-TRNA LIGASE
1	550	Hamap	MF_00126	Glutamine--tRNA ligase [glnS].
1	550	InterPro	IPR022861	Glutamine-tRNA ligase, bacterial
30	248	Gene3D	G3DSA:3.40.50.620	HUPs
30	248	InterPro	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold

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_A0A0H3GPY5	AlphaFold	—	—	full sequence	—	Viewing
ColabFold VK055_1830	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
1				0.933
5				0.398
2				0.366

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	17.79	0.808
2	3.76	0.145
3	2.84	0.089
4	2.57	0.073
5	1.46	0.02

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
2				0.231

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	17.27	0.8
2	4.81	0.214
3	2.35	0.061
4	1.65	0.027
5	1.25	0.012

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.

62 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
8X1	5V58	P07814	429.4 Da LogP -3.23 TPSA 203.8	1 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
91Y	5VAD	P07814	364.4 Da LogP 2.89 TPSA 84.0	✓ Ro5	✓ Clean	`c1ccc2c(c1)CC(C2)NC(=O)c3c(nccn3)NC(=O)C4CCCCC4`
ADN	4K87	P07814	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)…`
ANP	4HVC	P07814	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)…`
DTT	4H3S	P13188	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
GSU	2RE8	P00962	475.4 Da LogP -3.40 TPSA 255.1	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
HFG	4HVC	P07814	414.7 Da LogP 1.88 TPSA 84.2	✓ Ro5	✓ Clean	`c1c2c(cc(c1Cl)Br)N=CN(C2=O)CC(=O)C[C@@H]3[C@H](…`
QSI	1EUQ	P00962	474.5 Da LogP -4.00 TPSA 260.9	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`

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
P5A	P07814	9.22	443.4 Da LogP -2.84 TPSA 203.8	1 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
CHEMBL5279127	P07814	7.07	443.4 Da LogP -2.84 TPSA 203.8	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(=O)(=O)NC(=O)[C…`
CHEMBL5291357	P00962	6.55	461.4 Da LogP -2.25 TPSA 244.2	2 viol.	✓ Clean	`NC(=O)CCC(N)COP(=O)(O)OC[C@H]1O[C@@H](n2cnc3c(N…`
CHEMBL609187	P47897	6.55	597.4 Da LogP -5.24 TPSA 284.3	3 viol.	✓ Clean	`NC(=O)CCC(N)COP(=O)([O-])OC[C@H]1OC(n2cnc3c(N)n…`

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
ZINC1849658	1.000	414.7 Da LogP 1.88 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@@H]1NCCC[C@@H]1O)Cn1cnc2cc(Br)c(Cl)cc2c…`
ZINC1849659	1.000	414.7 Da LogP 1.88 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@@H]1NCCC[C@H]1O)Cn1cnc2cc(Br)c(Cl)cc2c1…`
ZINC1849660	1.000	414.7 Da LogP 1.88 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@H]1NCCC[C@H]1O)Cn1cnc2cc(Br)c(Cl)cc2c1=O`
ZINC5784191	1.000	414.7 Da LogP 1.88 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@H]1NCCC[C@@H]1O)Cn1cnc2cc(Br)c(Cl)cc2c1…`
ZINC1849460	0.927	414.7 Da LogP 1.88 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@H]1NCCC[C@H]1O)Cn1cnc2cc(Cl)c(Br)cc2c1=O`
ZINC168710640	0.877	474.5 Da LogP -4.00 TPSA 260.9	2 viol.	✓ Clean	`NC(=O)CC[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](…`
ZINC168710738	0.877	474.5 Da LogP -4.00 TPSA 260.9	2 viol.	✓ Clean	`NC(=O)CC[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](…`
ZINC1083817667	0.779	459.5 Da LogP -2.22 TPSA 217.8	1 viol.	✓ Clean	`CC(C)C[C@@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n…`
ZINC936069053	0.779	459.5 Da LogP -2.22 TPSA 217.8	1 viol.	✓ Clean	`CC(C)C[C@@H](N)C(=O)NS(=O)(=O)OC[C@@H]1O[C@H](n…`
ZINC936069043	0.729	459.5 Da LogP -2.22 TPSA 217.8	1 viol.	✓ Clean	`CC[C@@H](C)[C@@H](N)C(=O)NS(=O)(=O)OC[C@@H]1O[C…`
ZINC14967098	0.716	403.4 Da LogP -3.64 TPSA 217.8	1 viol.	✓ Clean	`NCC(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc…`
ZINC218033334	0.716	403.4 Da LogP -3.64 TPSA 217.8	1 viol.	✓ Clean	`NCC(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc…`
ZINC218033425	0.716	403.4 Da LogP -3.64 TPSA 217.8	1 viol.	✓ Clean	`NCC(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc…`
ZINC218033503	0.716	403.4 Da LogP -3.64 TPSA 217.8	1 viol.	✓ Clean	`NCC(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc…`
ZINC31475423	0.712	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC12360002	0.703	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	0.703	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	0.703	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	0.703	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	0.703	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	0.703	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	0.703	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.703	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	0.703	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.703	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	0.703	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC1560411656	0.698	413.7 Da LogP 2.43 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@@H]1NCCC[C]1O)Cn1cnc2cc(Br)c(Cl)cc2c1=O`
ZINC13518964	0.694	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515	0.694	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045	0.694	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158	0.694	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931	0.694	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.694	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.694	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.694	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.694	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.694	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.694	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442	0.694	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167	0.694	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC4096224	0.683	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850	0.682	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066	0.682	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786	0.682	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246	0.682	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC31516918	0.681	446.4 Da LogP -1.33 TPSA 218.2	1 viol.	✓ Clean	`CC(C)[C@H](N)C(=O)O[P@](=O)(O)OC[C@H]1O[C@@H](n…`
ZINC31260554	0.671	474.5 Da LogP -3.16 TPSA 264.4	2 viol.	✓ Clean	`NC(=O)CC[C@H](N)/C(O)=N/S(=O)(=O)OC[C@H]1O[C@@H…`
ZINC31976683	0.671	474.5 Da LogP -3.16 TPSA 264.4	2 viol.	✓ Clean	`NC(=O)CC[C@H](N)/C(O)=N/S(=O)(=O)OC[C@H]1O[C@@H…`
ZINC105372833	0.667	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837	0.667	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`

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.