Research workbench

Methionyl-tRNA synthetase from staphylococcus aureus complexed with L- met

Analyse Methionyl-tRNA synthetase from staphylococcus aureus complexed with L- met in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7WPK
Type: protein
Length: 512 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: Q5HII6
Ligands: MET
Pockets: 4 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methionine--tRNA ligase (EC 6.1.1.10)	protein	512	51% helix, 15% strand	Q5HII6

Ligands and binding sites

MET · Methionine · ligand · chains A

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

Pockets

4 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	373	0.68	0.81	44	MET
2	205	0.65	0.84	23	empty
3	147	0.47	0.77	18	empty
4	59	0.35	0.77	14	empty

Compared structures

7WPK · Methionyl-tRNA synthetase from Staphylococcus aureus complexed with L-Met · the same entry in another collection · chain A against A, TM-score 1.00
Q5HII6 · AlphaFold monomer V2.0 prediction for methionine--tRNA ligase (Q5HII6) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q5HII6
Elsewhere: RCSB PDB 7WPK · PDBe 7WPK · UniProt Q5HII6

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