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Crystal structure of the leurs editing domain of candida albicans mutant K510A

Analyse Crystal structure of the leurs editing domain of candida albicans mutant K510A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5AGH
Type: protein
Length: 245 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Potential cytosolic leucyl tRNA synthetase
EC: 6.1.1.4
UniProt: Q5A9A4
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Potential cytosolic leucyl tRNA synthetase (EC 6.1.1.4)	protein	245	36% helix, 25% strand	Q5A9A4

Ligands and binding sites

ACT · Acetate ion · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	308	0.72	0.85	32	ACT

Compared structures

5AGH · Crystal structure of the LeuRS editing domain of Candida albicans Mutant K510A · 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 Q5A9A4
Elsewhere: RCSB PDB 5AGH · PDBe 5AGH · UniProt Q5A9A4

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