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Crystal structure of the P.FALCIPARUM cytosolic leucyl- tRNA synthetase editing domain (space group P1)

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: 5FO4
Type: protein
Length: 619 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Leucyl tRNA synthase
EC: 6.1.1.4
UniProt: C6KT64
Pockets: 7 · 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 synthase (EC 6.1.1.4)	protein	302	40% helix, 23% strand	C6KT64
B	Leucyl tRNA synthase (EC 6.1.1.4)	protein	317	39% helix, 21% strand	C6KT64

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	347	0.74	0.85	39	empty
2	311	0.71	0.84	32	empty
3	228	0.56	0.78	33	empty
4	316	0.55	0.75	33	empty
5	121	0.44	0.77	15	empty

Interfaces

1 interface between chains.

A–B · 796 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

5FO4 · 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 5FO4 · PDBe 5FO4 · UniProt C6KT64

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