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Crystal structure of T. cruzi histidyl-tRNA synthetase in complex with N-(quinolin-3-YL)PROPANAMIDE (chem 1698)

Analyse Crystal structure of T. cruzi histidyl-tRNA synthetase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4YRS
Type: protein
Length: 418 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histidyl-tRNA synthetase
EC: 6.1.1.21
UniProt: Q4DA54
Ligands: HIS, 4JS
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histidyl-tRNA synthetase (EC 6.1.1.21)	protein	418	42% helix, 21% strand	Q4DA54

Ligands and binding sites

HIS · Histidine · ligand · chains A
4JS · N-(quinolin-3-yl)propanamide · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	510	0.67	0.78	48	HIS, 4JS
2	68	0.37	0.78	15	empty
3	101	0.35	0.74	22	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

4YRS · Crystal structure of T. cruzi Histidyl-tRNA synthetase in complex with… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q4DA54
Elsewhere: RCSB PDB 4YRS · PDBe 4YRS · UniProt Q4DA54

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