Protein target profile

KP13_01303

Valyl-tRNA synthetase

Genome: KpKP13 Gene: valS AHE46631.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GQW8

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Length 951

Pocket druggability 0.226

Direct ligand evidence 0 68 total records

Functional annotation 1 EC 9 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 (%): 50.0 Lower values reduce human off-target concern.
Human E-value: 4.33e-63
Gut microbiome similarity: 4.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 96.109 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: 93.31 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 0.226

Structure A0A0H3GQW8

Pocket Pocket 18

P2Rank 0.934

Structure A0A0H3GQW8

Pocket Pocket 1

ColabFold model

FPocket 0.289 · Pocket 14

P2Rank 0.941 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 222 / 4744 genomes with a hit

Prevalence 4.7%

Cross-references

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

Sequence

UniProt A0A0H3GQW8

Chemistry

ChEMBL CHEMBL605376 ChEMBL CHEMBL605592 ChEMBL CHEMBL125820 ChEMBL CHEMBL125075 ChEMBL CHEMBL332104 ChEMBL CHEMBL1163069 ChEMBL CHEMBL264002 ChEMBL CHEMBL333001 ChEMBL CHEMBL341331 ChEMBL CHEMBL126515 ChEMBL CHEMBL340359 ChEMBL CHEMBL123796 ChEMBL CHEMBL125221 ChEMBL CHEMBL538163 ChEMBL CHEMBL3989715

Sequence

Primary amino-acid sequence viewer.

MEKTYNPQDIEQPLYEHWEKQGYFKPNGDESQESFCIMIPPPNVTGSLHMGHAFQQTIMDTMIRYQRMQGKNTLWQAGTDHAGIATQMVVERKIAAEEGKTRHDYGRDAFIDKIWQWKAESGGTITRQMRRLGNSVDWERERFTMDEGLSNAVKEVFVRLYKEDLIYRGKRLVNWDPKLRTAISDLEVENRESKGSMWHIRYPLADGAKTADGKDYLVVATTRPETLLGDTGVAVNPEDPRYKDLIGKFVVLPLVNRRIPIVGDEHADMEKGTGCVKITPAHDFNDYEVGRRHQLPMINILTFDGDIRESAEVYDTKGNESDVYSSEIPAEFQKLERFAARKAVVAAVDALGLLEEIKPHDLTVPYGDRGGVVIEPMLTDQWYVRADVLAKPAVEAVENGDIQFVPKQYENMYFSWMRDIQDWCISRQLWWGHRIPAWYDNDGNVYVGRSEDEVRQENNLSADVALRQDEDVLDTWFSSALWTFSTLGWPENTDALRQFHPTSVMVSGFDIIFFWIARMIMMTMHFIKDENGKPQVPFKTVYMTGLIRDDEGQKMSKSKGNVIDPLDMVDGITLPELLEKRTGNMMQPQLADKIRKRTEKQFPNGIEPHGTDALRFTLAALASTGRDINWDMKRLEGYRNFCNKLWNASRFVLMNTEDQDCGFNGGEMVLSLADRWIIAEFNHTVKAYREALDNFRFDIAAGILYEFTWNQFCDWYLELTKPVMNGGSEAELRGTRHTLVTVLEGLLRLAHPIIPFITETIWQRVKAICGITADTIMLQPFPQYDASQVDDAALADTEWLKQAIVAVRNIRAEMNIAPGKPLELLLRGCSKEAERRVNDNRSFLLNLARLESITVLPADDKGPVSVTKIVDGAELLIPMAGLINKEDELARLAKEVAKIEGEIGRIESKLANEGFVARAPEAVIAKEREKLEGYAEAKAKLIEQQAVIAAL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

6.1.1.9

Gene Ontology (GO)

GO:0002161 The hydrolysis of an incorrectly aminoacylated tRNA.
GO:0006438 The process of coupling valine to valyl-tRNA, catalyzed by valyl-tRNA synthetase. The valyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a valine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
GO:0004812 Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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:0004832 Catalysis of the reaction: L-valine + ATP + tRNA(Val) = L-valyl-tRNA(Val) + AMP + diphosphate + 2 H+.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
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.

55 records

Show feature table

Start	End	DB	Term	Name
331	555	FunFam	G3DSA:3.40.50.620:FF:000146	Valine--tRNA ligase
344	555	Gene3D	G3DSA:3.40.50.620	HUPs
344	555	InterPro	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
1	949	Hamap	MF_02004	Valine--tRNA ligase [valS].
1	949	InterPro	IPR002303	Valine-tRNA ligase
579	817	Gene3D	G3DSA:1.10.730.10	-
642	899	SUPERFAMILY	SSF47323	Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases
642	899	InterPro	IPR009080	Aminoacyl-tRNA synthetase, class Ia, anticodon-binding
924	944	Coils	Coil	Coil
886	944	Pfam	PF10458	Valyl tRNA synthetase tRNA binding arm
886	944	InterPro	IPR019499	Valyl-tRNA synthetase, tRNA-binding arm
578	817	FunFam	G3DSA:1.10.730.10:FF:000007	Valine--tRNA ligase
877	948	FunFam	G3DSA:1.10.287.380:FF:000001	Valine--tRNA ligase
882	909	Coils	Coil	Coil
877	948	Gene3D	G3DSA:1.10.287.380	-
877	948	InterPro	IPR037118	Valyl-tRNA synthetase, tRNA-binding arm superfamily
191	365	SUPERFAMILY	SSF50677	ValRS/IleRS/LeuRS editing domain
191	365	InterPro	IPR009008	Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain
1	498	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
42	53	ProSitePatterns	PS00178	Aminoacyl-transfer RNA synthetases class-I signature.
42	53	InterPro	IPR001412	Aminoacyl-tRNA synthetase, class I, conserved site
2	200	Gene3D	G3DSA:3.40.50.620	HUPs
2	200	InterPro	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
674	824	Pfam	PF08264	Anticodon-binding domain of tRNA ligase
674	824	InterPro	IPR013155	Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding
33	630	CDD	cd00817	ValRS_core
1	940	PANTHER	PTHR11946	VALYL-TRNA SYNTHETASES
1	940	InterPro	IPR002303	Valine-tRNA ligase
14	631	Pfam	PF00133	tRNA synthetases class I (I, L, M and V)
14	631	InterPro	IPR002300	Aminoacyl-tRNA synthetase, class Ia
1	641	SUPERFAMILY	SSF52374	Nucleotidylyl transferase
884	947	SUPERFAMILY	SSF46589	tRNA-binding arm
884	947	InterPro	IPR010978	Class I and II aminoacyl-tRNA synthetase, tRNA-binding arm
499	517	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
518	951	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
630	764	CDD	cd07962	Anticodon_Ia_Val
630	764	InterPro	IPR033705	Valyl tRNA synthetase, anticodon-binding domain
1	932	NCBIfam	TIGR00422	valine--tRNA ligase
1	932	InterPro	IPR002303	Valine-tRNA ligase
242	343	Gene3D	G3DSA:3.90.740.10	-
242	343	InterPro	IPR009008	Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain
201	241	Gene3D	G3DSA:3.90.740.10	-
201	241	InterPro	IPR009008	Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain
469	490	PRINTS	PR00986	Valyl-tRNA synthetase signature
469	490	InterPro	IPR002303	Valine-tRNA ligase
35	46	PRINTS	PR00986	Valyl-tRNA synthetase signature
35	46	InterPro	IPR002303	Valine-tRNA ligase
236	253	PRINTS	PR00986	Valyl-tRNA synthetase signature
236	253	InterPro	IPR002303	Valine-tRNA ligase
500	518	PRINTS	PR00986	Valyl-tRNA synthetase signature
500	518	InterPro	IPR002303	Valine-tRNA ligase
369	382	PRINTS	PR00986	Valyl-tRNA synthetase signature
369	382	InterPro	IPR002303	Valine-tRNA ligase
204	355	FunFam	G3DSA:3.90.740.10:FF:000021	Valine--tRNA ligase
3	200	FunFam	G3DSA:3.40.50.620:FF:000032	Valine--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 #18

0.226

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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

0.934

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Surrounding area

Site 2 P2Rank #2

0.64

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Surrounding area

Site 3 P2Rank #3

0.403

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Surrounding area

Site 4 P2Rank #4

0.269

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Surrounding area

Site 5 P2Rank #5

0.133

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Surrounding area

Residue sets

UniProt: Binding site:557-557

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.941

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Surrounding area

Site 2 P2Rank #2

0.63

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Surrounding area

Site 3 P2Rank #3

0.587

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Surrounding area

Site 4 P2Rank #4

0.34

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Surrounding area

Site 5 P2Rank #5

0.106

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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_A0A0H3GQW8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01303	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.

68 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 18 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 15 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ILA PDB via homolog 458.5 Da · LogP -2.65 · TPSA 220.6 Open detail RCSB PDB

MRC PDB via homolog Detail RCSB PDB

VAA PDB via homolog Detail RCSB PDB

CHEMBL605376 ChEMBL via homolog · pchembl 7.85 (~14.1 nM) Detail ChEMBL

CHEMBL605592 ChEMBL via homolog · pchembl 7.41 (~38.9 nM) Detail ChEMBL

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
ILA RCSB PDB	1JZQ	P56690	458.5 Da LogP -2.65 TPSA 220.6	2 viol.	✓ Clean	`CC[C@H](C)[C@@H](C(=O)NS(=O)(=O)NC[C@@H]1[C@H](…`
MRC RCSB PDB	1JZS	P56690	500.6 Da LogP 2.59 TPSA 146.1	1 viol.	✓ Clean	`C[C@H]([C@H]1[C@@H](O1)C[C@H]2CO[C@H]([C@@H]([C…`
VAA RCSB PDB	1GAX	P96142	444.5 Da LogP -3.04 TPSA 220.6	2 viol.	✓ Clean	`CC(C)[C@@H](C(=O)NS(=O)(=O)NC[C@@H]1[C@H]([C@H]…`

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
CHEMBL605376 ChEMBL	P41252	7.85 ~14.1 nM	585.4 Da LogP -1.62 TPSA 217.8	2 viol.	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1OC(n2c…`
CHEMBL605592 ChEMBL	P41252	7.41 ~38.9 nM	483.5 Da LogP -2.24 TPSA 217.8	1 viol.	✓ Clean	`C#Cc1nc(N)c2ncn(C3O[C@H](COS(=O)(=O)NC(=O)[C@@H…`
CHEMBL125820 ChEMBL	P41972	7.40 ~39.8 nM	513.6 Da LogP 0.84 TPSA 161.1	1 viol.	✓ Clean	`CCC(C)[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](c2…`
CHEMBL125075 ChEMBL	P41972	7.30 ~50.1 nM	515.6 Da LogP 0.73 TPSA 170.3	2 viol.	✓ Clean	`CCC(C)[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](c2…`
CHEMBL332104 ChEMBL	P41972	7.05 ~89.1 nM	513.6 Da LogP 0.84 TPSA 161.1	1 viol.	✓ Clean	`CC(C)C[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](c2…`
CHEMBL1163069 ChEMBL	P41252	7.01 ~97.7 nM	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@@H…`
CHEMBL264002 ChEMBL	P41252	7.00 ~100.0 nM	485.6 Da LogP 0.72 TPSA 161.1	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H…`
CHEMBL333001 ChEMBL	P41972	7.00 ~100.0 nM	515.6 Da LogP 0.73 TPSA 170.3	2 viol.	✓ Clean	`CCC(C)[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](c2…`
CHEMBL341331 ChEMBL	P41972	7.00 ~100.0 nM	605.7 Da LogP 2.63 TPSA 170.3	2 viol.	✓ Clean	`CC(C)C[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](c2…`
CHEMBL126515 ChEMBL	P41972	6.92 ~120.2 nM	605.7 Da LogP 2.63 TPSA 170.3	2 viol.	✓ Clean	`CCC(C)[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](c2…`
CHEMBL340359 ChEMBL	P41972	6.89 ~128.8 nM	565.7 Da LogP 1.88 TPSA 170.3	2 viol.	✓ Clean	`CCC(C)[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](c2…`
CHEMBL123796 ChEMBL	P41972	6.62 ~239.9 nM	500.6 Da LogP 0.19 TPSA 198.0	2 viol.	✓ Clean	`CCC(C)[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](c2…`
CHEMBL125221 ChEMBL	P41972	6.57 ~269.2 nM	577.7 Da LogP 2.52 TPSA 170.3	2 viol.	✓ Clean	`CCC(C)[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](c2…`
CHEMBL538163 ChEMBL	P41972	6.52 ~302.0 nM	515.6 Da LogP 0.73 TPSA 170.3	2 viol.	✓ Clean	`CCC(C)[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](c2…`
CHEMBL3989715 ChEMBL	P41972	—	1075.3 Da LogP 0.49 TPSA 360.8	3 viol.	✓ Clean	`C/C(=C\C(=O)OCCCCCCCCC(=O)[O-])C[C@@H]1OC[C@H](…`

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
ZINC77312672 ZINC	0.846	498.6 Da LogP 2.37 TPSA 146.1	✓ Ro5	✓ Clean	`C/C(=C\C(=O)OCCCC/C=C/CCC(=O)O)C[C@@H]1OC[C@H](…`
ZINC67665217 ZINC	0.839	456.6 Da LogP 3.14 TPSA 108.8	✓ Ro5	✓ Clean	`CCCCCCCCOC(=O)/C=C(\C)C[C@@H]1OC[C@@H](C[C@@H]2…`
ZINC67665219 ZINC	0.839	456.6 Da LogP 3.14 TPSA 108.8	✓ Ro5	✓ Clean	`CCCCCCCCOC(=O)/C=C(\C)C[C@@H]1OC[C@H](C[C@@H]2O…`
ZINC936069043 ZINC	0.765	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…`
ZINC1560411707 ZINC	0.700	499.6 Da LogP 2.76 TPSA 146.1	✓ Ro5	✓ Clean	`C/C(=C\C(=O)OCCCCCCCCC(=O)O)C[C]1OC[C@H](C[C@@H…`
ZINC38803309 ZINC	0.691	484.6 Da LogP 3.38 TPSA 133.5	✓ Ro5	✓ Clean	`C/C(=C\C(=O)OCCCCCCCCC(=O)O)C[C@@H]1OC[C@H](C/C…`
ZINC4824159 ZINC	0.683	344.4 Da LogP -2.42 TPSA 165.5	✓ Ro5	✓ Clean	`CS(=O)(=O)NC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@…`
ZINC4824161 ZINC	0.683	344.4 Da LogP -2.42 TPSA 165.5	✓ Ro5	✓ Clean	`CS(=O)(=O)NC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC4824165 ZINC	0.683	344.4 Da LogP -2.42 TPSA 165.5	✓ Ro5	✓ Clean	`CS(=O)(=O)NC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@…`
ZINC4824166 ZINC	0.683	344.4 Da LogP -2.42 TPSA 165.5	✓ Ro5	✓ Clean	`CS(=O)(=O)NC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC13488353 ZINC	0.639	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@…`
ZINC1083817667 ZINC	0.600	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	0.600	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…`
ZINC12405780 ZINC	0.567	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	0.567	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@@H]…`
ZINC13547650 ZINC	0.567	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	0.567	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	0.567	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	0.567	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	0.567	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CC(=O)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](…`
ZINC79460727 ZINC	0.567	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	0.567	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@H](…`
ZINC14967098 ZINC	0.562	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	0.562	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	0.562	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	0.562	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…`
ZINC24951137 ZINC	0.554	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…`
ZINC168710640 ZINC	0.551	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	0.551	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](…`
ZINC13522400 ZINC	0.549	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	0.549	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…`
ZINC1582675 ZINC	0.549	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486730 ZINC	0.549	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486734 ZINC	0.549	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`
ZINC5486740 ZINC	0.549	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`
ZINC49014951 ZINC	0.542	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	0.542	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…`
ZINC5139067 ZINC	0.540	283.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CS)[C@@H](O)[C@H]1O`
ZINC31516918 ZINC	0.539	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…`
ZINC4776036 ZINC	0.536	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CCOC(=O)[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O…`
ZINC4776037 ZINC	0.536	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CCOC(=O)[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](…`
ZINC4776038 ZINC	0.536	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CCOC(=O)[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O…`
ZINC4776039 ZINC	0.536	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CCOC(=O)[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](…`
ZINC2047403 ZINC	0.531	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H]1O`
ZINC2047673 ZINC	0.531	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@@H]1O`
ZINC2169830 ZINC	0.531	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC4773848 ZINC	0.531	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H]…`
ZINC77981211 ZINC	0.531	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@H]…`
ZINC82228511 ZINC	0.531	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@H]1O`
ZINC970363 ZINC	0.531	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`

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_01303

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