Protein target profile

KP13_03562

Glutamyl-tRNA synthetase

Genome: KpKP13 Gene: AHE43367.1 gltX 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GTA8

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Length 472

Pocket druggability 0.394

Direct ligand evidence 0 63 total records

Functional annotation 1 EC 10 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: Hit
Human identity (%): 36.364 Lower values reduce human off-target concern.
Human E-value: 3.23e-65
Gut microbiome similarity: 4.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 95.319 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 95.97 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.394

Structure A0A0H3GTA8

Pocket Pocket 3

P2Rank 0.907

Structure A0A0H3GTA8

Pocket Pocket 1

ColabFold model

FPocket 0.477 · Pocket 3

P2Rank 0.876 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 191 / 4744 genomes with a hit

Prevalence 4.0%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GTA8

Chemistry

ChEMBL P5A ChEMBL CHEMBL5279127 ChEMBL CHEMBL5291357

Sequence

Primary amino-acid sequence viewer.

MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLQWDEGPYFQTKRFDRYNNVIDEMLEAGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHHADDEPCVVRFANPQEGSVIFDDQIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMAITHVIRGEDHINNTPRQINILKALNAPVPVYAHVSMINGDDGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFTREEMIEFFSLGAVSKSASAFNTDKLLWLNHHYINTLPAEYVATHLQWHIEQENIDTRNGPQLAELVKLLGERCKTLKEMAQSCRYFYEEFSEFDADAAKKHLRPVARQPLEVVRDKLAAISDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKSRSVDRINKALAFIAEREGQAS

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

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
363	471	Gene3D	G3DSA:1.10.10.350	-
363	471	InterPro	IPR020751	Aminoacyl-tRNA synthetase, class I, anticodon-binding domain, subdomain 2
3	298	SUPERFAMILY	SSF52374	Nucleotidylyl transferase
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
1	314	FunFam	G3DSA:3.40.50.620:FF:000007	Glutamate--tRNA ligase
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
2	313	CDD	cd00808	GluRS_core
2	313	InterPro	IPR033910	Glutamyl-tRNA synthetase
326	461	Pfam	PF19269	Anticodon binding domain
326	461	InterPro	IPR045462	Aminoacyl-tRNA synthetase, class I, anticodon-binding
9	20	ProSitePatterns	PS00178	Aminoacyl-transfer RNA synthetases class-I signature.
9	20	InterPro	IPR001412	Aminoacyl-tRNA synthetase, class I, conserved site
1	313	Gene3D	G3DSA:3.40.50.620	HUPs
1	313	InterPro	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
363	471	FunFam	G3DSA:1.10.10.350:FF:000001	Glutamate--tRNA ligase
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
2	461	Hamap	MF_00022	Glutamate--tRNA ligase [gltX].
2	461	InterPro	IPR004527	Glutamate-tRNA ligase, bacterial/mitochondrial
2	463	NCBIfam	TIGR00464	glutamate--tRNA ligase
2	463	InterPro	IPR004527	Glutamate-tRNA ligase, bacterial/mitochondrial
2	462	PANTHER	PTHR43311	GLUTAMATE--TRNA LIGASE

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #3

0.394

Likely same site as P2Rank 4 3.2 Å 6 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #2

0.269

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.907

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Surrounding area

Site 2 P2Rank #2

0.091

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Surrounding area

Site 3 P2Rank #3

0.068

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Surrounding area

Site 4 P2Rank #4

0.019

Likely same site as FPocket 3 3.2 Å 6 shared residues 100% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.01

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Surrounding area

Residue sets

UniProt: Binding site:100-100

UniProt: Binding site:125-125

UniProt: Binding site:127-127

UniProt: Binding site:240-240

UniProt: Binding site:98-98

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #3

0.477

Likely same site as P2Rank 4 3.9 Å 5 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #1

0.404

Likely same site as P2Rank 1 0.3 Å 26 shared residues 96% of smaller site

Unusual size

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Surrounding area

Site 3 FPocket #27

0.246

Unusual size

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Surrounding area

Site 4 FPocket #18

0.232

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.876

Likely same site as FPocket 1 0.3 Å 26 shared residues 96% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.072

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Surrounding area

Site 3 P2Rank #3

0.014

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Surrounding area

Site 4 P2Rank #4

0.012

Likely same site as FPocket 3 3.9 Å 5 shared residues 100% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.002

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3GTA8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03562	ColabFold	—	—	full sequence	—	Loaded

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

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 13 records from similar proteins

Structural ligands 10 0 loaded crystals

Measured bioactivity 3 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

8X1 PDB via homolog 429.4 Da · LogP -3.23 · TPSA 203.8 Open detail RCSB PDB

91Y PDB via homolog Detail RCSB PDB

ADN PDB via homolog Detail RCSB PDB

ANP PDB via homolog Detail RCSB PDB

DTT PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, 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 RCSB PDB	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 RCSB PDB	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 RCSB PDB	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 RCSB PDB	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 RCSB PDB	4H3S	P13188	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
GAU RCSB PDB	2CV1	P27000	133.1 Da LogP -0.83 TPSA 83.5	✓ Ro5	✓ Clean	`C(CC(=O)O)[C@@H](CO)N`
GOM RCSB PDB	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 RCSB PDB	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 RCSB PDB	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 RCSB PDB	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 ChEMBL	P07814	9.22 ~0.6 nM	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 ChEMBL	P07814	7.07 ~85.1 nM	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 ChEMBL	P00962	6.55 ~281.8 nM	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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.

KP13_03562

Target candidate with partial support; inspect missing evidence before prioritizing.

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Chemistry

Sequence

Functional annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence