KpKP13 Protein target profile

Tyrosyl-tRNA synthetase

Accession: KP13_05164

Gene: AHE44283.1 tyrS 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GTN6

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Length 428

Pocket druggability (P2Rank · AlphaFold DB model) 0.909

Direct ligand evidence 0 65 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.42. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.91. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for 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 (%): 42.041 Lower values reduce human off-target concern.
Human E-value: 1.38e-53
Gut microbiome similarity: 5.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 95.519 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 94.45 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) 0.909

Structure A0A0H3GTN6

Pocket Pocket 1

Druggability (FPocket) 0.419

Structure A0A0H3GTN6

Pocket Pocket 9

ColabFold model

P2Rank 0.925 · Pocket 1

FPocket 0.491 · Pocket 18

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 238 / 4744 genomes with a hit

Prevalence 5.0%

Sequence

Primary amino-acid sequence viewer.

MENLMASSNLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPTADSLHLGHLVPLLCLKRFQQAGHKPVALVGGATGLIGDPSFKAAERKLNTEDTVQEWVDKIRKQVAPFLDFDCGDNSAIAANNYDWFGSMNVLTFLRDIGKHFSVNQMINKEAVKQRLNRDDQGISFTEFSYNLLQGYDFACLNKLHGVALQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKTEGGAVWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMDIAEINALEEEDKNSGKAPRAQYVLAEQVTRLVHGEEGLEAAKRITESLFNGNLSDLSEADFEQLAQDGVPMIEMEKGADLLQALVDSELQPSRGQARKTVASNAVTINGEKQADPEYVFSDSDRLFGRYTLLRRGKKNYCLVCWK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

6.1.1.1

Gene Ontology (GO)

GO:0004812 Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP.
GO:0004831 Catalysis of the reaction: L-tyrosine + ATP + tRNA(Tyr) = L-tyrosyl-tRNA(Tyr) + AMP + diphosphate + 2 H+.
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:0006437 The process of coupling tyrosine to tyrosyl-tRNA, catalyzed by tyrosyl-tRNA synthetase. The tyrosyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a tyrosine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
GO:0003723 Binding to an RNA molecule or a portion thereof.
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.
GO:0042803 Binding to an identical protein to form a homodimer.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

34 records

Show feature table

Start	End	DB	Term	Name
331	427	SUPERFAMILY	SSF55174	Alpha-L RNA-binding motif
192	214	PRINTS	PR01040	Tyrosyl-tRNA synthetase signature
192	214	InterPro	IPR002307	Tyrosine-tRNA ligase
50	72	PRINTS	PR01040	Tyrosyl-tRNA synthetase signature
50	72	InterPro	IPR002307	Tyrosine-tRNA ligase
171	186	PRINTS	PR01040	Tyrosyl-tRNA synthetase signature
171	186	InterPro	IPR002307	Tyrosine-tRNA ligase
225	237	PRINTS	PR01040	Tyrosyl-tRNA synthetase signature
225	237	InterPro	IPR002307	Tyrosine-tRNA ligase
35	332	Pfam	PF00579	tRNA synthetases class I (W and Y)
35	332	InterPro	IPR002305	Aminoacyl-tRNA synthetase, class Ic
337	428	FunFam	G3DSA:3.10.290.10:FF:000007	Tyrosine--tRNA ligase
5	231	Gene3D	G3DSA:3.40.50.620	HUPs
5	231	InterPro	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
337	428	Gene3D	G3DSA:3.10.290.10	-
337	428	InterPro	IPR036986	RNA-binding S4 domain superfamily
8	427	Hamap	MF_02006	Tyrosine--tRNA ligase [tyrS].
8	427	InterPro	IPR024107	Tyrosine-tRNA ligase, bacterial-type, type 1
38	314	CDD	cd00805	TyrRS_core
38	314	InterPro	IPR002307	Tyrosine-tRNA ligase
232	336	Gene3D	G3DSA:1.10.240.10	-
363	408	CDD	cd00165	S4
361	418	ProSiteProfiles	PS50889	S4 RNA-binding domain profile.
362	423	SMART	SM00363	s4_6
362	423	InterPro	IPR002942	RNA-binding S4 domain
46	56	ProSitePatterns	PS00178	Aminoacyl-transfer RNA synthetases class-I signature.
46	56	InterPro	IPR001412	Aminoacyl-tRNA synthetase, class I, conserved site
6	427	PANTHER	PTHR11766	TYROSYL-TRNA SYNTHETASE
6	427	InterPro	IPR024088	Tyrosine-tRNA ligase, bacterial-type
5	231	FunFam	G3DSA:3.40.50.620:FF:000008	Tyrosine--tRNA ligase
8	332	SUPERFAMILY	SSF52374	Nucleotidylyl transferase
232	334	FunFam	G3DSA:1.10.240.10:FF:000001	Tyrosine--tRNA ligase
6	428	NCBIfam	TIGR00234	tyrosine--tRNA ligase
6	428	InterPro	IPR002307	Tyrosine-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

0.909

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Surrounding area

Pocket 2 P2Rank #2

0.312

Likely same site as FPocket 9 1.6 Å 9 shared residues 82% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.065

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Surrounding area

Pocket 4 P2Rank #4

0.028

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Surrounding area

Pocket 5 P2Rank #5

0.027

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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 #9

0.419

Likely same site as P2Rank 2 1.6 Å 9 shared residues 82% of smaller site

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Surrounding area

Residue sets

UniProt: Binding site:179-179

UniProt: Binding site:183-183

UniProt: Binding site:242-242

UniProt: Binding site:41-41

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.925

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Surrounding area

Pocket 2 P2Rank #2

0.294

Likely same site as FPocket 25 1.3 Å 7 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.066

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Surrounding area

Pocket 4 P2Rank #4

0.055

Likely same site as FPocket 18 1.2 Å 10 shared residues 100% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.017

Likely same site as FPocket 3 1.4 Å 10 shared residues 91% of smaller site

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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 #18

0.491

Likely same site as P2Rank 4 1.2 Å 10 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #3

0.379

Likely same site as P2Rank 5 1.4 Å 10 shared residues 91% of smaller site

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Surrounding area

Pocket 3 FPocket #25

0.215

Likely same site as P2Rank 2 1.3 Å 7 shared residues 100% of smaller site

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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_A0A0H3GTN6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_05164	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.

65 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 15 records from similar proteins

Structural ligands 8 0 loaded crystals

Measured bioactivity 7 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AZY PDB via homolog 222.2 Da · LogP 1.29 · TPSA 132.3 Open detail RCSB PDB

IYR PDB via homolog Detail RCSB PDB

TYE PDB via homolog Detail RCSB PDB

TYS PDB via homolog Detail RCSB PDB

Y3U 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
AZY RCSB PDB	2YXN	P0AGJ9	222.2 Da LogP 1.29 TPSA 132.3	✓ Ro5	Alert	`c1cc(c(cc1C[C@@H](C(=O)O)N)N=[N+]=[N-])O`
IYR RCSB PDB	1WQ3	P0AGJ9	307.1 Da LogP 0.95 TPSA 83.5	✓ Ro5	✓ Clean	`c1cc(c(cc1C[C@@H](C(=O)O)N)I)O`
TYE RCSB PDB	1H3E	P83453	167.2 Da LogP 0.25 TPSA 66.5	✓ Ro5	✓ Clean	`c1cc(ccc1C[C@@H](CO)N)O`
TYS RCSB PDB	6WN2	P0AGJ9	261.3 Da LogP -0.18 TPSA 126.9	✓ Ro5	✓ Clean	`c1cc(ccc1C[C@@H](C(=O)O)N)OS(=O)(=O)O`
Y3U RCSB PDB	6HB7	P0AGJ9	500.5 Da LogP -3.18 TPSA 212.4	2 viol.	✓ Clean	`CN1C(=O)C=CN(C1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…`
YSA RCSB PDB	1VBM	P0AGJ9	509.5 Da LogP -2.32 TPSA 238.0	3 viol.	✓ Clean	`c1cc(ccc1C[C@@H](C(=O)NS(=O)(=O)OC[C@@H]2[C@H](…`
YSC RCSB PDB	6HB5	P0AGJ9	485.5 Da LogP -2.90 TPSA 229.3	2 viol.	✓ Clean	`c1cc(ccc1C[C@@H](C(=O)NS(=O)(=O)OC[C@@H]2[C@H](…`
YSU RCSB PDB	6HB6	P0AGJ9	486.5 Da LogP -3.19 TPSA 223.3	2 viol.	✓ Clean	`c1cc(ccc1C[C@@H](C(=O)NS(=O)(=O)OC[C@@H]2[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
CHEMBL4208126 ChEMBL	P0AGJ9	7.52 ~30.2 nM	508.5 Da LogP -1.71 TPSA 225.1	3 viol.	✓ Clean	`Nc1nccc2c1ncn2[C@@H]1O[C@H](COS(=O)(=O)NC(=O)[C…`
CHEMBL1163069 ChEMBL	P0AGJ9	—	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…`
CHEMBL3265242 ChEMBL	P0AGJ9	—	435.5 Da LogP -2.80 TPSA 209.1	1 viol.	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H…`
CHEMBL3265243 ChEMBL	P0AGJ9	—	436.4 Da LogP -3.09 TPSA 203.0	1 viol.	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H…`
CHEMBL4467328 ChEMBL	P0AGJ9	—	436.4 Da LogP -3.09 TPSA 203.0	1 viol.	✓ Clean	`CC(C)C[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n2…`
HQ5 ChEMBL	P0AGJ9	—	435.5 Da LogP -2.80 TPSA 209.1	1 viol.	✓ Clean	`CC(C)C[C@@H](C(=O)NS(=O)(=O)OC[C@@H]1[C@H]([C@H…`
LSS ChEMBL	P0AGJ9	—	459.5 Da LogP -2.22 TPSA 217.8	1 viol.	✓ Clean	`CC(C)C[C@@H](C(=O)NS(=O)(=O)OC[C@@H]1[C@H]([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
ZINC1083817667 ZINC	1.000	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…`
ZINC14824920 ZINC	1.000	261.3 Da LogP -0.18 TPSA 126.9	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(OS(=O)(=O)O)cc1)C(=O)O`
ZINC1575 ZINC	1.000	307.1 Da LogP 0.95 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)c(I)c1)C(=O)O`
ZINC2556660 ZINC	1.000	261.3 Da LogP -0.18 TPSA 126.9	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(OS(=O)(=O)O)cc1)C(=O)O`
ZINC391106 ZINC	1.000	307.1 Da LogP 0.95 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(O)c(I)c1)C(=O)O`
ZINC936069043 ZINC	1.000	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…`
ZINC936069053 ZINC	1.000	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…`
ZINC403598 ZINC	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC403599 ZINC	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC168710640 ZINC	0.779	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	0.779	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](…`
ZINC39351856 ZINC	0.741	328.4 Da LogP 1.26 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1)C…`
ZINC13488353 ZINC	0.735	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@…`
ZINC14967098 ZINC	0.727	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	0.727	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	0.727	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	0.727	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…`
ZINC33821383 ZINC	0.725	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](…`
ZINC6092925 ZINC	0.718	399.2 Da LogP 2.74 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Oc2ccc(O)c(I)c2)cc1)C(=O)O`
ZINC2512061 ZINC	0.706	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@@H](Cc1ccc(O)c(-c2cc(C[C@H](N)C(=O)O)ccc2O)…`
ZINC6091882 ZINC	0.706	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@@H](Cc1ccc(O)c(-c2cc(C[C@@H](N)C(=O)O)ccc2O…`
ZINC6091894 ZINC	0.706	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@H](Cc1ccc(O)c(-c2cc(C[C@@H](N)C(=O)O)ccc2O)…`
ZINC13354682 ZINC	0.703	321.1 Da LogP 1.04 TPSA 72.5	✓ Ro5	✓ Clean	`COC(=O)[C@H](N)Cc1ccc(O)c(I)c1`
ZINC13354686 ZINC	0.703	321.1 Da LogP 1.04 TPSA 72.5	✓ Ro5	✓ Clean	`COC(=O)[C@@H](N)Cc1ccc(O)c(I)c1`
ZINC202880439 ZINC	0.703	320.1 Da LogP 0.61 TPSA 75.4	✓ Ro5	✓ Clean	`CNC(=O)[C@H](N)Cc1ccc(O)c(I)c1`
ZINC202880453 ZINC	0.703	320.1 Da LogP 0.61 TPSA 75.4	✓ Ro5	✓ Clean	`CNC(=O)[C@@H](N)Cc1ccc(O)c(I)c1`
ZINC238594226 ZINC	0.694	309.1 Da LogP 1.38 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(F)c(I)c1)C(=O)O`
ZINC238609587 ZINC	0.694	325.5 Da LogP 1.90 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Cl)c(I)c1)C(=O)O`
ZINC238611106 ZINC	0.694	309.1 Da LogP 1.38 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(F)c(I)c1)C(=O)O`
ZINC32333 ZINC	0.690	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC32334 ZINC	0.690	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC3679925 ZINC	0.690	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(I)cc1)C(=O)O`
ZINC391104 ZINC	0.690	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(I)cc1)C(=O)O`
ZINC4202286 ZINC	0.690	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC4202287 ZINC	0.690	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC6092920 ZINC	0.690	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC6506146 ZINC	0.690	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC34319489 ZINC	0.688	231.3 Da LogP 1.50 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc2cc(O)ccc2c1)C(=O)O`
ZINC34319490 ZINC	0.688	231.3 Da LogP 1.50 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc2cc(O)ccc2c1)C(=O)O`
ZINC3861723 ZINC	0.676	433.0 Da LogP 1.56 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1cc(I)c(O)c(I)c1)C(=O)O`
ZINC3875424 ZINC	0.676	433.0 Da LogP 1.56 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1cc(I)c(O)c(I)c1)C(=O)O`
ZINC113264413 ZINC	0.667	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC14982778 ZINC	0.667	207.2 Da LogP 0.84 TPSA 80.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC2575475 ZINC	0.667	238.2 Da LogP -0.54 TPSA 112.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)cc1)C(=O)NCC(=O)O`
ZINC2575618 ZINC	0.667	208.2 Da LogP -0.26 TPSA 106.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC402814 ZINC	0.667	215.6 Da LogP 1.00 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(O)c(Cl)c1)C(=O)O`
ZINC4241956 ZINC	0.667	208.2 Da LogP -0.26 TPSA 106.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC6091875 ZINC	0.667	260.1 Da LogP 1.11 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)c(Br)c1)C(=O)O`
ZINC6091892 ZINC	0.667	260.1 Da LogP 1.11 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(O)c(Br)c1)C(=O)O`
ZINC79460727 ZINC	0.667	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@H](…`

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.

Sequence

UniProt A0A0H3GTN6

Chemistry

ChEMBL CHEMBL4208126 ChEMBL CHEMBL1163069 ChEMBL CHEMBL3265242 ChEMBL CHEMBL3265243 ChEMBL CHEMBL4467328 ChEMBL HQ5 ChEMBL LSS