KpATCC43816 Protein target profile

cysteine--tRNA ligase

Accession: VK055_2065

Gene: cysS AIK80670.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A0H3GT08

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Length 461

Pocket druggability (P2Rank · AlphaFold DB model) 0.925

Metabolic reactions 2

Chokepoint Yes

Direct ligand evidence 0 79 total records

Functional annotation 1 EC 9 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

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

Main supporting evidence

Metabolic chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.93. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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 (%): 55.952 Lower values reduce human off-target concern.
Human E-value: 1.66e-25
Gut microbiome similarity: 6.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 95.879 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 93.4 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.925

Structure A0A0H3GT08

Pocket Pocket 1

Druggability (FPocket) 0.222

Structure A0A0H3GT08

Pocket Pocket 1

ColabFold model

P2Rank 0.947 · Pocket 1

FPocket 0.413 · Pocket 4

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 310 / 4744 genomes with a hit

Prevalence 6.5%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Attractive metabolic target: catalyzes a producing chokepoint reaction in Aminoacyl-tRNA biosynthesis, no isoenzyme backup detected.

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MLKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVSFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANENGESFVALVDRMIAEMHKDFDALNILRPDSEPRATHHIAEIIEITEQLIAKGHAYVADNGDVMFDVPTDPNYGLLSRQDLDQLQAGARVDVVDVKRNPMDFVLWKMSKEGEPSWPSPWGAGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIAQSTCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETIRYFLMSGHYRSQLNYSEENLKQARSALERLYTALRGTDKSVDAAGGEAFEARFIEAMDDDFNTPEAYSVLFDMAREVNRLKTEDAAAANAMAAHLRKLAAVLGLLEQEPEAFLQSGAQVDDAEVAEIESLIQQRLDARKAKDWAAADAARDRLNEMGIVLEDGPQGTTWRRK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

6.1.1.16

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0004817 Catalysis of the reaction: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys).
GO:0004812 Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP.
GO:0006423 The process of coupling cysteine to cysteinyl-tRNA, catalyzed by cysteinyl-tRNA synthetase. A cysteinyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a cysteine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
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: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:0008270 Binding to a zinc ion (Zn).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

30 records

Show feature table

Start	End	DB	Term	Name
341	402	Pfam	PF09190	DALR domain
341	402	InterPro	IPR015273	Cysteinyl-tRNA synthetase, class Ia, DALR
1	313	SUPERFAMILY	SSF52374	Nucleotidylyl transferase
3	305	CDD	cd00672	CysRS_core
3	305	InterPro	IPR032678	tRNA synthetases class I, catalytic domain
303	461	FunFam	G3DSA:1.20.120.1910:FF:000001	Cysteine--tRNA ligase
306	460	CDD	cd07963	Anticodon_Ia_Cys
2	460	NCBIfam	TIGR00435	cysteine--tRNA ligase
2	460	InterPro	IPR015803	Cysteine-tRNA ligase
341	402	SMART	SM00840	dalr_2_4
2	460	PANTHER	PTHR10890	CYSTEINYL-TRNA SYNTHETASE
2	460	InterPro	IPR024909	Cysteinyl-tRNA synthetase/mycothiol ligase
2	461	Hamap	MF_00041	Cysteine--tRNA ligase [cysS].
2	461	InterPro	IPR015803	Cysteine-tRNA ligase
303	461	Gene3D	G3DSA:1.20.120.1910	-
1	302	Gene3D	G3DSA:3.40.50.620	HUPs
1	302	InterPro	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
15	313	Pfam	PF01406	tRNA synthetases class I (C) catalytic domain
15	313	InterPro	IPR032678	tRNA synthetases class I, catalytic domain
222	243	PRINTS	PR00983	Cysteinyl-tRNA synthetase signature
222	243	InterPro	IPR024909	Cysteinyl-tRNA synthetase/mycothiol ligase
25	36	PRINTS	PR00983	Cysteinyl-tRNA synthetase signature
25	36	InterPro	IPR024909	Cysteinyl-tRNA synthetase/mycothiol ligase
61	70	PRINTS	PR00983	Cysteinyl-tRNA synthetase signature
61	70	InterPro	IPR024909	Cysteinyl-tRNA synthetase/mycothiol ligase
191	209	PRINTS	PR00983	Cysteinyl-tRNA synthetase signature
191	209	InterPro	IPR024909	Cysteinyl-tRNA synthetase/mycothiol ligase
316	460	SUPERFAMILY	SSF47323	Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases
316	460	InterPro	IPR009080	Aminoacyl-tRNA synthetase, class Ia, anticodon-binding
1	303	FunFam	G3DSA:3.40.50.620:FF:000009	Cysteine--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 · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.925

Likely same site as FPocket 1 0.6 Å 26 shared residues 96% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.194

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Surrounding area

Pocket 3 P2Rank #3

0.109

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Surrounding area

Pocket 4 P2Rank #4

0.066

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Surrounding area

Pocket 5 P2Rank #5

0.047

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.222 Unusual size

Likely same site as P2Rank 1 0.6 Å 26 shared residues 96% of smaller site

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Surrounding area

Residue sets

UniProt: Binding site:209-209

UniProt: Binding site:234-234

UniProt: Binding site:238-238

UniProt: Binding site:269-269

UniProt: Binding site:28-28

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.947

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Surrounding area

Pocket 2 P2Rank #2

0.116

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Surrounding area

Pocket 3 P2Rank #3

0.091

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Surrounding area

Pocket 4 P2Rank #4

0.084

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Surrounding area

Pocket 5 P2Rank #5

0.026

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Surrounding area

Residue sets

UniProt: Binding site:209-209

UniProt: Binding site:234-234

UniProt: Binding site:238-238

UniProt: Binding site:269-269

UniProt: Binding site:28-28

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_A0A0H3GT08	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2065	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.

79 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 29 records from similar proteins

Structural ligands 1 0 loaded crystals

Measured bioactivity 28 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

PG5 PDB via homolog 178.2 Da · LogP 0.31 · TPSA 36.9 Open detail RCSB PDB

U7S ChEMBL via homolog · pchembl 10.40 (~0.0 nM) Detail ChEMBL

CHEMBL362023 ChEMBL via homolog · pchembl 8.48 (~3.3 nM) Detail ChEMBL

CHEMBL424799 ChEMBL via homolog · pchembl 8.42 (~3.8 nM) Detail ChEMBL

CHEMBL359928 ChEMBL via homolog · pchembl 8.41 (~3.9 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
PG5 RCSB PDB	6UJD	A0A1T3F4R2	178.2 Da LogP 0.31 TPSA 36.9	✓ Ro5	✓ Clean	`COCCOCCOCCOC`

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
U7S ChEMBL	Q8NY00	10.40 ~0.0 nM	450.4 Da LogP 5.19 TPSA 56.9	1 viol.	✓ Clean	`Cc1c(sc(c1Br)C(=C)F)CNCCCNC2=CC(=O)c3ccccc3N2`
CHEMBL362023 ChEMBL	Q8NY00	8.48 ~3.3 nM	467.4 Da LogP 4.16 TPSA 88.5	✓ Ro5	✓ Clean	`CCOc1c(Br)cc(OC)cc1CNCCCNc1nc(O)c2sccc2n1`
CHEMBL424799 ChEMBL	Q8NY00	8.42 ~3.8 nM	437.8 Da LogP 4.97 TPSA 62.0	✓ Ro5	✓ Clean	`CCOc1c(Br)cc(Cl)cc1CNCCCNc1nc2ccccc2[nH]1`
CHEMBL359928 ChEMBL	Q8NY00	8.41 ~3.9 nM	472.2 Da LogP 4.10 TPSA 69.8	✓ Ro5	✓ Clean	`O=c1nc(NCCCNCc2cc(Br)cc(Br)c2)[nH]c2ccsc12`
CHEMBL182767 ChEMBL	Q8NY00	8.31 ~4.9 nM	516.3 Da LogP 4.91 TPSA 79.3	1 viol.	✓ Clean	`CCOc1c(Br)cc(Br)cc1CNCCCNc1nc(O)c2sccc2n1`
CHEMBL182960 ChEMBL	Q8NY00	8.30 ~5.0 nM	439.2 Da LogP 4.03 TPSA 65.6	✓ Ro5	✓ Clean	`Brc1cc(Br)cc(CNCCCNc2nc3ccc[nH]c-3n2)c1`
CHEMBL2096779 ChEMBL	Q8NY00	8.20 ~6.3 nM	480.2 Da LogP 4.38 TPSA 77.7	✓ Ro5	✓ Clean	`Brc1cc(Br)c2c(c1)[C@H](NCCCNc1nc3ccc[nH]c-3n1)C…`
CHEMBL368020 ChEMBL	Q8NY00	8.15 ~7.1 nM	461.4 Da LogP 4.10 TPSA 88.5	✓ Ro5	✓ Clean	`CCOc1c(Br)cc(OC)cc1CNCCCNc1nc(O)c2ccccc2n1`
CHEMBL425169 ChEMBL	Q8NY00	8.09 ~8.1 nM	466.2 Da LogP 4.45 TPSA 70.1	✓ Ro5	✓ Clean	`Oc1nc(NCCCNCc2cc(Br)cc(Br)c2)nc2ccccc12`
CHEMBL426613 ChEMBL	Q8NY00	8.09 ~8.1 nM	462.8 Da LogP 4.70 TPSA 82.1	✓ Ro5	✓ Clean	`Oc1nc(NCCCNC2CCNc3c(Cl)cc(Br)cc32)nc2ccccc12`
CHEMBL182414 ChEMBL	Q8NY00	8.01 ~9.8 nM	510.2 Da LogP 4.85 TPSA 79.3	1 viol.	✓ Clean	`CCOc1c(Br)cc(Br)cc1CNCCCNc1nc(O)c2ccccc2n1`
CHEMBL182225 ChEMBL	Q8NY00	7.96 ~11.0 nM	480.2 Da LogP 4.43 TPSA 77.7	✓ Ro5	✓ Clean	`Brc1cc(Br)c2c(c1)C(NCCCNc1nc3ncccc3[nH]1)CCN2`
YY3 ChEMBL	P49589	7.92 ~12.0 nM	499.6 Da LogP 4.51 TPSA 87.6	✓ Ro5	✓ Clean	`Cn1cc(c2c1cccc2)c3ccnc(n3)Nc4cc(c(cc4OC)N(C)CCN…`
CHEMBL361649 ChEMBL	Q8NY00	7.89 ~12.9 nM	479.2 Da LogP 5.04 TPSA 64.8	1 viol.	✓ Clean	`Brc1cc(Br)c2c(c1)C(NCCCNc1nc3ccccc3[nH]1)CCN2`
CHEMBL361788 ChEMBL	Q8NY00	7.89 ~12.9 nM	513.3 Da LogP 4.87 TPSA 82.1	1 viol.	✓ Clean	`Oc1nc(NCCCNC2CCNc3c(Br)cc(Br)cc32)nc2ccsc12`
CHEMBL183110 ChEMBL	Q8NY00	7.80 ~15.8 nM	475.4 Da LogP 4.68 TPSA 64.8	✓ Ro5	✓ Clean	`CCc1cc(I)c2c(c1)C(NCCCNc1nc3ccccc3[nH]1)CCN2`
CHEMBL180309 ChEMBL	Q8NY00	7.77 ~17.0 nM	482.2 Da LogP 5.08 TPSA 62.0	1 viol.	✓ Clean	`CCOc1c(Br)cc(Br)cc1CNCCCNc1nc2ccccc2[nH]1`
CHEMBL185486 ChEMBL	Q8NY00	7.77 ~17.0 nM	433.4 Da LogP 4.32 TPSA 71.2	✓ Ro5	✓ Clean	`CCOc1c(Br)cc(OC)cc1CNCCCNc1nc2ccccc2[nH]1`
CHEMBL425706 ChEMBL	Q8NY00	7.77 ~17.0 nM	503.4 Da LogP 4.45 TPSA 82.1	1 viol.	✓ Clean	`CCc1cc(I)c2c(c1)C(NCCCNc1nc(O)c3ccccc3n1)CCN2`
CHEMBL182821 ChEMBL	Q8NY00	7.75 ~17.8 nM	476.4 Da LogP 4.03 TPSA 77.7	✓ Ro5	✓ Clean	`CCc1cc(I)c2c(c1)C(NCCCNc1nc3ccc[nH]c-3n1)CCN2`
CHEMBL182263 ChEMBL	Q8NY00	7.54 ~28.8 nM	438.2 Da LogP 4.68 TPSA 52.7	✓ Ro5	✓ Clean	`Brc1cc(Br)cc(CNCCCNc2nc3ccccc3[nH]2)c1`
5CA ChEMBL	P9WJM9	7.31 ~49.0 nM	449.5 Da LogP -3.34 TPSA 217.8	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
CHEMBL185520 ChEMBL	Q8NY00	7.27 ~53.7 nM	462.2 Da LogP 5.16 TPSA 63.6	1 viol.	✓ Clean	`N#Cc1c(NCCCNCc2cc(Br)cc(Br)c2)[nH]c2ccccc12`
CHEMBL181657 ChEMBL	Q8NY00	7.00 ~100.0 nM	394.7 Da LogP 5.79 TPSA 37.0	1 viol.	✓ Clean	`Clc1cc(Cl)c(Cl)c(CNCCCNc2ccc3ccccc3n2)c1`
CHEMBL182650 ChEMBL	Q8NY00	6.48 ~331.1 nM	441.2 Da LogP 4.51 TPSA 53.2	✓ Ro5	✓ Clean	`O=C(NCCCNCc1cc(Br)cc(Br)c1)Nc1ccccc1`
CHEMBL2087361 ChEMBL	P49589	6.19 ~645.7 nM	391.4 Da LogP 3.16 TPSA 74.7	✓ Ro5	✓ Clean	`C#Cc1cccc(Nc2ncnc3cc4c(cc23)OCCOCCOCCO4)c1`
CHEMBL359723 ChEMBL	Q8NY00	6.00 ~1.0 µM	411.7 Da LogP 5.35 TPSA 54.3	1 viol.	✓ Clean	`O=c1cc(NCCCNCc2cc(Cl)cc(Cl)c2Cl)oc2ccccc12`
CHEMBL1795953 ChEMBL	P9WJM9	—	564.2 Da LogP 6.05 TPSA 75.7	2 viol.	✓ Clean	`CN(CCCNC(=O)c1ccc2c(c1)N(Cc1cccc(Cl)c1)C(=O)c1c…`

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
ZINC1692489 ZINC	1.000	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC43207566 ZINC	1.000	391.4 Da LogP 3.16 TPSA 74.7	✓ Ro5	✓ Clean	`C#Cc1cccc(Nc2ncnc3cc4c(cc23)OCCOCCOCCO4)c1`
ZINC4530388 ZINC	1.000	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5701172 ZINC	1.000	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861 ZINC	1.000	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC98023177 ZINC	1.000	499.6 Da LogP 4.51 TPSA 87.5	✓ Ro5	✓ Clean	`C=CC(=O)Nc1cc(Nc2nccc(-c3cn(C)c4ccccc34)n2)c(OC…`
ZINC146550081 ZINC	0.880	485.6 Da LogP 4.17 TPSA 96.3	✓ Ro5	✓ Clean	`C=CC(=O)Nc1cc(Nc2nccc(-c3cn(C)c4ccccc34)n2)c(OC…`
ZINC2382328959 ZINC	0.849	487.6 Da LogP 4.34 TPSA 87.5	✓ Ro5	✓ Clean	`COc1cc(N(C)CCN(C)C)c(NC(C)=O)cc1Nc1nccc(-c2cn(C…`
ZINC1083817667 ZINC	0.841	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	0.841	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…`
ZINC168710640 ZINC	0.828	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	0.828	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](…`
ZINC1911936317 ZINC	0.818	486.6 Da LogP 4.45 TPSA 93.5	✓ Ro5	✓ Clean	`C=CC(=O)Nc1cc(Nc2nccc(-c3cn(C)c4ccccc34)n2)c(OC…`
ZINC936069043 ZINC	0.785	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	0.774	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	0.774	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	0.774	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	0.774	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…`
ZINC147059673 ZINC	0.756	485.6 Da LogP 4.50 TPSA 98.4	✓ Ro5	✓ Clean	`C=CC(=O)Nc1cc(Nc2nccc(-c3c[nH]c4ccccc34)n2)c(OC…`
ZINC34764844 ZINC	0.733	206.3 Da LogP 1.09 TPSA 36.9	✓ Ro5	✓ Clean	`CCCOCCOCCOCCOC`
ZINC146451979 ZINC	0.724	445.6 Da LogP 3.97 TPSA 84.5	✓ Ro5	✓ Clean	`COc1cc(N(C)CCN(C)C)c(N)cc1Nc1nccc(-c2cn(C)c3ccc…`
ZINC12405780 ZINC	0.712	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	0.712	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	0.712	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	0.712	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@H](…`
ZINC146568246 ZINC	0.700	475.6 Da LogP 4.29 TPSA 101.6	✓ Ro5	✓ Clean	`COc1cc(N(C)CCN(C)C)c([N+](=O)[O-])cc1Nc1nccc(-c…`
ZINC140264883 ZINC	0.688	223.3 Da LogP -0.43 TPSA 72.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCON`
ZINC143705779 ZINC	0.688	443.5 Da LogP -0.34 TPSA 118.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCON`
ZINC1580161 ZINC	0.688	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118 ZINC	0.688	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257 ZINC	0.688	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC33358855 ZINC	0.688	207.3 Da LogP -0.36 TPSA 62.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCN`
ZINC34317654 ZINC	0.688	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44076059 ZINC	0.688	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44583772 ZINC	0.688	356.5 Da LogP 0.66 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCS`
ZINC5024003 ZINC	0.688	251.3 Da LogP -0.34 TPSA 72.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCN`
ZINC5210101 ZINC	0.688	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC575432090 ZINC	0.688	355.4 Da LogP -0.38 TPSA 99.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCON`
ZINC575432265 ZINC	0.688	399.5 Da LogP -0.36 TPSA 109.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCON`
ZINC5997860 ZINC	0.688	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC71254558 ZINC	0.688	444.6 Da LogP 0.70 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC71254563 ZINC	0.688	488.6 Da LogP 0.71 TPSA 92.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC83253927 ZINC	0.688	400.5 Da LogP 0.68 TPSA 73.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC83253930 ZINC	0.688	224.3 Da LogP 0.61 TPSA 36.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCS`
ZINC83253936 ZINC	0.688	383.5 Da LogP -0.29 TPSA 99.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCN`
ZINC90556279 ZINC	0.688	295.4 Da LogP -0.33 TPSA 81.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCN`
ZINC90556280 ZINC	0.688	339.4 Da LogP -0.31 TPSA 90.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCN`
ZINC90556286 ZINC	0.688	312.4 Da LogP 0.65 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCS`
ZINC90556287 ZINC	0.688	268.4 Da LogP 0.63 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCS`
ZINC96503353 ZINC	0.688	471.6 Da LogP -0.26 TPSA 118.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCN`

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.

Cross-references

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

cysteine--tRNA ligase

Promising target candidate with multiple supporting evidence streams.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways