Protein target profile

HT085_RS00335

tyrosine--tRNA ligase

Genome: NZ_AP023069.1 Gene: TUM19854C_00560 NCTC11421_02832 tyrS 3D evidence: AlphaFold DB model UniProt A0A1D3GBP6

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Length 431

Direct ligand evidence 0 65 total records

Functional annotation 1 EC 6 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
Gut microbiome off-target: Hit

Essentiality

Essential (DEG): Y

Localization

Localization: Cytoplasmic

Binding-site evidence

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 Medium

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MSVIQDLQSRGLIAQTTDIEALDALLNEQKIALYCGFDPTADSLHIGHLLPVLALRRFQQAGHTPIALVGGATGMIGDPSFKAAERSLNSAETVAGWVGSIRSQLTPFLSFEGGNAAIMANNADWFGSMNCLDFLRDIGKHFSVNAMLNKESVKQRIDRDGAGISFTEFAYSLLQGYDFAELNKRHGAVLEIGGSDQWGNITAGIDLTRRLNQKQVFGLTLPLVTKSDGTKFGKTEGGAVWLNAKKTSPYQFYQFWLKVADADVYKFLKYFTFLSIEEIGVIEAKDKASGSKPEAQRILAEEMTRLIHGEEALAAAQRISESLFAEDQSRLTESDFEQLALDGLPAFEVSDGINAVEALVKTGLAASNKEARGFVNAKAVLLNGKPAEANNPNHAAERPDDAYLLIGEYKRFGKYTILRRGKRNHALLVWK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

6.1.1.1

Gene Ontology (GO)

GO:0004831 Catalysis of the reaction: L-tyrosine + ATP + tRNA(Tyr) = L-tyrosyl-tRNA(Tyr) + AMP + diphosphate + 2 H+.
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: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.

32 records

Show feature table

Start	End	DB	Term	Name
359	388	CDD	cd00165	S4
1	430	Hamap	MF_02006	Tyrosine--tRNA ligase [tyrS].
1	430	InterPro	IPR024107	Tyrosine-tRNA ligase, bacterial-type, type 1
224	327	FunFam	G3DSA:1.10.240.10:FF:000001	Tyrosine--tRNA ligase
39	49	ProSitePatterns	PS00178	Aminoacyl-transfer RNA synthetases class-I signature.
39	49	InterPro	IPR001412	Aminoacyl-tRNA synthetase, class I, conserved site
324	430	SUPERFAMILY	SSF55174	Alpha-L RNA-binding motif
1	223	Gene3D	G3DSA:3.40.50.620	HUPs
1	223	InterPro	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
2	324	SUPERFAMILY	SSF52374	Nucleotidylyl transferase
2	429	PANTHER	PTHR11766	TYROSYL-TRNA SYNTHETASE
2	429	InterPro	IPR024088	Tyrosine-tRNA ligase, bacterial-type
331	431	FunFam	G3DSA:3.10.290.10:FF:000027	Tyrosine--tRNA ligase
4	430	NCBIfam	TIGR00234	tyrosine--tRNA ligase
4	430	InterPro	IPR002307	Tyrosine-tRNA ligase
224	330	Gene3D	G3DSA:1.10.240.10	-
331	431	Gene3D	G3DSA:3.10.290.10	-
331	431	InterPro	IPR036986	RNA-binding S4 domain superfamily
1	223	FunFam	G3DSA:3.40.50.620:FF:000008	Tyrosine--tRNA ligase
28	324	Pfam	PF00579	tRNA synthetases class I (W and Y)
28	324	InterPro	IPR002305	Aminoacyl-tRNA synthetase, class Ic
31	306	CDD	cd00805	TyrRS_core
31	306	InterPro	IPR002307	Tyrosine-tRNA ligase
353	422	ProSiteProfiles	PS50889	S4 RNA-binding domain profile.
217	229	PRINTS	PR01040	Tyrosyl-tRNA synthetase signature
217	229	InterPro	IPR002307	Tyrosine-tRNA ligase
184	206	PRINTS	PR01040	Tyrosyl-tRNA synthetase signature
184	206	InterPro	IPR002307	Tyrosine-tRNA ligase
43	65	PRINTS	PR01040	Tyrosyl-tRNA synthetase signature
43	65	InterPro	IPR002307	Tyrosine-tRNA ligase
163	178	PRINTS	PR01040	Tyrosyl-tRNA synthetase signature
163	178	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 · FPocket

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

Site 1 FPocket #4

0.535

Likely same site as P2Rank 2 3.4 Å 8 shared residues 73% of smaller site

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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

0.891

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Surrounding area

Site 2 P2Rank #2

0.207

Likely same site as FPocket 4 3.4 Å 8 shared residues 73% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.019

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Surrounding area

Site 4 P2Rank #4

0.015

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Surrounding area

Site 5 P2Rank #5

0.012

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Surrounding area

All structural evidence 0 experimental · 1 predicted

Structural evidence

0 + 1

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 HT085_RS00335	AlphaFold DB	—	—	full sequence	—	Viewing

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…`
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](…`
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`
ZINC2512061 ZINC	0.677	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	0.677	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	0.677	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)…`
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`
ZINC113264415 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`
ZINC12405780 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]…`
ZINC12502832 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]…`
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`
ZINC14982780 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`
ZINC1569734 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`
ZINC2244337 ZINC	0.667	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC2244338 ZINC	0.667	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC2505456 ZINC	0.667	210.2 Da LogP 0.72 TPSA 94.8	✓ Ro5	✓ Clean	`O=C(O)C(Cc1ccc(O)cc1)C(=O)O`
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`
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`
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](…`
ZINC79460732 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](…`
ZINC20268092 ZINC	0.654	230.1 Da LogP 1.31 TPSA 46.2	✓ Ro5	✓ Clean	`N[C@@H](CO)Cc1ccc(Br)cc1`
ZINC20268094 ZINC	0.654	230.1 Da LogP 1.31 TPSA 46.2	✓ Ro5	✓ Clean	`N[C@H](CO)Cc1ccc(Br)cc1`
ZINC44466880 ZINC	0.654	277.1 Da LogP 1.15 TPSA 46.2	✓ Ro5	✓ Clean	`N[C@H](CO)Cc1ccc(I)cc1`
ZINC44466883 ZINC	0.654	277.1 Da LogP 1.15 TPSA 46.2	✓ Ro5	✓ Clean	`N[C@@H](CO)Cc1ccc(I)cc1`
ZINC2004481 ZINC	0.647	344.4 Da LogP 0.78 TPSA 132.9	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1ccc(O)cc1)…`
ZINC2392306 ZINC	0.645	221.3 Da LogP 1.94 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC3679865 ZINC	0.645	207.3 Da LogP 1.76 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC44284738 ZINC	0.645	255.3 Da LogP 2.62 TPSA 63.3	✓ Ro5	✓ Clean	`Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1`

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.

HT085_RS00335

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

Binding-site evidence

Sequence

Functional annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence