MolNFT v1 · #120527 · protein

Crystal structure of the C-terminal domain of methionyl-tRNA synthetase (metrs-C) in nanoarchaeum equitans

5H34 · Methionine-tRNA ligase: “Crystal structure of the C-terminal domain of methionyl-tRNA synthetase (metrs-C) in nanoarchaeum equitans”. X-ray diffraction, 2 pockets (best druggability 0.51). MolNFT v1 #120527 on GenesisL1: 3D…

PDB: 5H34
Type: protein
Length: 223 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methionine-tRNA ligase
EC: 6.1.1.10
UniProt: Q74MZ1
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methionine-tRNA ligase (EC 6.1.1.10)	protein	111	8% helix, 44% strand	Q74MZ1
B	Methionine-tRNA ligase (EC 6.1.1.10)	protein	112	8% helix, 44% strand	Q74MZ1

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	168	0.51	0.78	25	empty
2	143	0.49	0.78	24	empty

Interfaces

1 interface between chains.

A–B · 2178 Å² buried · 41 hydrogen bonds · protein-protein

Compared structures

5H34 · Crystal structure of the C-terminal domain of methionyl-tRNA synthetase (MetRS-C) in… · the same entry in another collection · chain A against A, TM-score 1.00
Q74MZ1 · AlphaFold monomer V2.0 prediction for methionine--tRNA ligase (Q74MZ1) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q74MZ1
Elsewhere: RCSB PDB 5H34 · PDBe 5H34 · UniProt Q74MZ1

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