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Crystal structure of the P.FALCIPARUM cytosolic leucyl-tRNA synthetase editing domain (space group P21)

Analyse Crystal structure of the P.FALCIPARUM cytosolic leucyl-tRNA synthetase editing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FOC
Type: protein
Length: 597 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Leucyl-tRNA synthetase
EC: 6.1.1.4
UniProt: C6KT64
Pockets: 5 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Leucyl-tRNA synthetase (EC 6.1.1.4)	protein	297	39% helix, 22% strand	C6KT64
B	Leucyl-tRNA synthetase (EC 6.1.1.4)	protein	300	39% helix, 22% strand	C6KT64

Pockets

5 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	647	0.74	0.80	65	empty
2	331	0.71	0.84	34	empty
3	126	0.49	0.79	19	empty
4	56	0.41	0.81	16	empty
5	69	0.40	0.79	16	empty

Interfaces

1 interface between chains.

A–B · 356 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

5FOC · Crystal structure of the P.falciparum cytosolic leucyl-tRNA synthetase editing domain… · 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 C6KT64
Elsewhere: RCSB PDB 5FOC · PDBe 5FOC · UniProt C6KT64

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