Protein profile

VK055_4762

glutamate--tRNA ligase

Genome: KpATCC43816

Gene: gltX AIK83292.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GTA8

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Amino acids 472

Annotations 11

Features 32

PDB binders 10

Druggability 0.394

Overview

Basic information about this protein and its source genome.

Accession: VK055_4762
Assembly: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene: gltX AIK83292.1
Status: annotated
Amino acids: 472
Structure source: AlphaFold + ColabFold

6.1.1.17

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: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. GO:0004818 Catalysis of the reaction: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). GO:0008270 Binding to a zinc ion (Zn). GO:0004812 Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 36.364
Human E-value: 3.48e-65
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 95.532
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 95.9

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 0.394

Structure A0A0H3GTA8

Pocket Pocket 3

P2Rank 0.907

Structure A0A0H3GTA8

Pocket Pocket 1

ColabFold model

FPocket 0.53 · Pocket 4

P2Rank 0.866 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 192 / 4744 genomes with a hit

Normalized 0.04

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

6.1.1.17

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: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.
GO:0004818 Catalysis of the reaction: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).
GO:0008270 Binding to a zinc ion (Zn).
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:0000049 Binding to a transfer RNA.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Sequence Features

Domain/signature hits from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
326	461	Pfam	PF19269	Anticodon binding domain
326	461	InterPro	IPR045462	Aminoacyl-tRNA synthetase, class I, anticodon-binding
2	462	PANTHER	PTHR43311	GLUTAMATE--TRNA LIGASE
363	471	Gene3D	G3DSA:1.10.10.350	-
363	471	InterPro	IPR020751	Aminoacyl-tRNA synthetase, class I, anticodon-binding domain, subdomain 2
1	313	Gene3D	G3DSA:3.40.50.620	HUPs
1	313	InterPro	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
2	463	NCBIfam	TIGR00464	glutamate--tRNA ligase
2	463	InterPro	IPR004527	Glutamate-tRNA ligase, bacterial/mitochondrial
6	18	PRINTS	PR00987	Glutamyl-tRNA synthetase signature
6	18	InterPro	IPR000924	Glutamyl/glutaminyl-tRNA synthetase
179	189	PRINTS	PR00987	Glutamyl-tRNA synthetase signature
179	189	InterPro	IPR000924	Glutamyl/glutaminyl-tRNA synthetase
20	31	PRINTS	PR00987	Glutamyl-tRNA synthetase signature
20	31	InterPro	IPR000924	Glutamyl/glutaminyl-tRNA synthetase
195	203	PRINTS	PR00987	Glutamyl-tRNA synthetase signature
195	203	InterPro	IPR000924	Glutamyl/glutaminyl-tRNA synthetase
35	48	PRINTS	PR00987	Glutamyl-tRNA synthetase signature
35	48	InterPro	IPR000924	Glutamyl/glutaminyl-tRNA synthetase
2	313	CDD	cd00808	GluRS_core
2	313	InterPro	IPR033910	Glutamyl-tRNA synthetase
3	298	SUPERFAMILY	SSF52374	Nucleotidylyl transferase
2	461	Hamap	MF_00022	Glutamate--tRNA ligase [gltX].
2	461	InterPro	IPR004527	Glutamate-tRNA ligase, bacterial/mitochondrial
9	20	ProSitePatterns	PS00178	Aminoacyl-transfer RNA synthetases class-I signature.
9	20	InterPro	IPR001412	Aminoacyl-tRNA synthetase, class I, conserved site
2	305	Pfam	PF00749	tRNA synthetases class I (E and Q), catalytic domain
2	305	InterPro	IPR020058	Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domain
299	461	SUPERFAMILY	SSF48163	An anticodon-binding domain of class I aminoacyl-tRNA synthetases
299	461	InterPro	IPR008925	Aminoacyl-tRNA synthetase, class I, anticodon-binding superfamily
363	471	FunFam	G3DSA:1.10.10.350:FF:000001	Glutamate--tRNA ligase
1	314	FunFam	G3DSA:3.40.50.620:FF:000007	Glutamate--tRNA ligase

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_A0A0H3GTA8	AlphaFold	—	—	full sequence	—	Viewing
ColabFold VK055_4762	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
2				0.269
1				0.117
4				0.012
31				0.0

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	31.04	0.907
2	3.28	0.091
3	2.77	0.068
4	1.56	0.019
5	1.24	0.01

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
7				0.263
1				0.165
3				0.002
26				0.001

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	25.53	0.866
2	2.13	0.041
3	1.38	0.014
4	1.28	0.011
5	1.15	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.

63 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`
GAU	2CV1	P27000	133.1 Da LogP -0.83 TPSA 83.5	✓ Ro5	✓ Clean	`C(CC(=O)O)[C@@H](CO)N`
GOM	1N78	P27000	461.3 Da LogP -4.33 TPSA 245.7	1 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
GSU	2CV2	P27000	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…`

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…`
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`
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…`
ZINC1571579	0.667	301.3 Da LogP 0.47 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@@H]1NCCC[C@@H]1O)Cn1cnc2ccccc2c1=O`
ZINC1571580	0.667	301.3 Da LogP 0.47 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@@H]1NCCC[C@H]1O)Cn1cnc2ccccc2c1=O`
ZINC1571581	0.667	301.3 Da LogP 0.47 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@H]1NCCC[C@H]1O)Cn1cnc2ccccc2c1=O`
ZINC5641945	0.667	301.3 Da LogP 0.47 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@H]1NCCC[C@@H]1O)Cn1cnc2ccccc2c1=O`
ZINC12405780	0.656	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@@H]…`
ZINC12502832	0.656	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@@H]…`
ZINC79460727	0.656	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@H](…`
ZINC79460732	0.656	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@H](…`
ZINC2390999	0.655	275.3 Da LogP -1.99 TPSA 172.8	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC14967079	0.653	461.4 Da LogP -2.95 TPSA 258.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(=O)(=O)/N=C(\O)…`
ZINC4830518	0.648	395.4 Da LogP -2.66 TPSA 211.7	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](NC(=O)[C@…`
ZINC4830519	0.648	395.4 Da LogP -2.66 TPSA 211.7	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](NC(=O)[C…`
ZINC4830520	0.648	395.4 Da LogP -2.66 TPSA 211.7	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](NC(=O)[C@…`
ZINC4830521	0.648	395.4 Da LogP -2.66 TPSA 211.7	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](NC(=O)[C…`
ZINC1560404579	0.615	412.7 Da LogP 2.92 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(CC1=C(O)CCCN1)Cn1cnc2cc(Br)c(Cl)cc2c1=O`
ZINC24951137	0.611	417.4 Da LogP -2.41 TPSA 221.3	1 viol.	✓ Clean	`C[C@H](N)/C(O)=N/S(=O)(=O)OC[C@H]1O[C@@H](n2cnc…`
ZINC33821383	0.600	459.5 Da LogP -1.38 TPSA 221.3	1 viol.	✓ Clean	`CC(C)C[C@H](N)/C(O)=N/S(=O)(=O)OC[C@H]1O[C@@H](…`
ZINC49014951	0.600	416.4 Da LogP -2.76 TPSA 216.8	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CS(=O)(=O)CC[C@H](N)…`
ZINC49014955	0.600	416.4 Da LogP -2.76 TPSA 216.8	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CS(=O)(=O)CC[C@@H](N…`
ZINC1574270	0.597	421.4 Da LogP -0.26 TPSA 162.7	1 viol.	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@@H]2O[C@H](n3cnc4c(N)ncnc4…`
ZINC3861767	0.597	421.4 Da LogP -0.26 TPSA 162.7	1 viol.	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@H]2O[C@@H](n3cnc4c(N)ncnc4…`
ZINC13488353	0.587	459.5 Da LogP -1.38 TPSA 221.3	1 viol.	✓ Clean	`CC[C@H](C)[C@H](N)/C(O)=N/S(=O)(=O)OC[C@H]1O[C@…`
ZINC2391099	0.586	274.3 Da LogP -2.59 TPSA 178.6	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC13522400	0.586	400.4 Da LogP -2.42 TPSA 199.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[S@](=O)CC[C@H](N)…`
ZINC13522403	0.586	400.4 Da LogP -2.42 TPSA 199.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[S@@](=O)CC[C@H](N…`
ZINC13547650	0.582	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CC(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)…`
ZINC4823971	0.582	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CC(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O…`
ZINC4823975	0.582	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CC(=O)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](…`
ZINC4823980	0.582	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CC(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O…`
ZINC4823984	0.582	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CC(=O)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](…`
ZINC13522378	0.580	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)O)[…`
ZINC256828117	0.580	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)O)[…`
ZINC256828118	0.580	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)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.