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The mutant structure of the human glycyl-tRNA synthetase E71G

Analyse The mutant structure of the human glycyl-tRNA synthetase E71G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KQE
Type: protein
Length: 597 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycine--tRNA ligase
EC: 6.1.1.14
UniProt: P41250
Pockets: 7 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycine--tRNA ligase (EC 6.1.1.14)	protein	597	37% helix, 24% strand	P41250

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

7 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	1172	0.73	0.76	93	empty
2	127	0.43	0.76	22	empty
3	126	0.41	0.75	21	empty
4	92	0.39	0.76	15	empty
5	63	0.37	0.79	19	empty

Compared structures

4KQE · The mutant structure of the human glycyl-tRNA synthetase E71G · the same entry in another collection · chain A against A, TM-score 1.00
P41250 · AlphaFold monomer V2.0 prediction for glycine--tRNA ligase (P41250) · a predicted model of the same protein · chain A against A, TM-score 0.88

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 P41250
Elsewhere: RCSB PDB 4KQE · PDBe 4KQE · UniProt P41250

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