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Structure of the escherichia COLI methionyl-tRNA synthetase variant VI298 complexed with methionine

Analyse Structure of the escherichia COLI methionyl-tRNA synthetase variant VI298… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SPQ
Type: protein
Length: 544 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methionine--tRNA ligase
EC: 6.1.1.10
UniProt: A0A0F3U9S7
Ligands: MET, ZN
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methionine--tRNA ligase (EC 6.1.1.10)	protein	544	51% helix, 17% strand	A0A0F3U9S7

Ligands and binding sites

MET · Methionine · ligand · chains A
ZN · Zinc ion · metal · chains A
GOL · Glycerol · additive · 4 copies · chains A
CIT · Citric acid · additive · 2 copies · chains A

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

Pockets

2 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	345	0.63	0.79	32	MET
2	163	0.50	0.78	34	CIT

Compared structures

6SPQ · Structure of the Escherichia coli methionyl-tRNA synthetase variant VI298 complexed with… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A0A0F3U9S7
Elsewhere: RCSB PDB 6SPQ · PDBe 6SPQ · UniProt A0A0F3U9S7

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