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Crystal structure of leishmania major prolyl-tRNA synthetase (lmprs)

Analyse Crystal structure of leishmania major prolyl-tRNA synthetase (lmprs) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5XIL
Type: protein
Length: 445 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative prolyl-tRNA synthetase
EC: 6.1.1.5, 6.1.1.7
UniProt: Q4QDS0
Ligands: MG, ZN
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative prolyl-tRNA synthetase (EC 6.1.1.5, 6.1.1.7)	protein	445	40% helix, 27% strand	Q4QDS0

Ligands and binding sites

MG · Magnesium ion · metal · 3 copies · chains A
ZN · Zinc ion · metal · chains A
ACT · Acetate ion · additive · 3 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	277	0.56	0.77	40	empty
2	147	0.54	0.81	23	empty
3	62	0.30	0.74	18	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5XIL · Crystal Structure of Leishmania major Prolyl-tRNA Synthetase (LmPRS) · 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 Q4QDS0
Elsewhere: RCSB PDB 5XIL · PDBe 5XIL · UniProt Q4QDS0

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