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Crystal structure of apo form (free-state) mycobacterium tuberculosis methionyl-tRNA synthetase

Analyse Crystal structure of apo form (free-state) mycobacterium tuberculosis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5XGQ
Type: protein
Length: 991 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: A5U150
Pockets: 9 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Methionine-tRNA ligase (EC 6.1.1.10)	protein	496	51% helix, 15% strand	A5U150
A	Methionine-tRNA ligase (EC 6.1.1.10)	protein	495	51% helix, 15% strand	A5U150

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	509	0.67	0.78	56	empty
2	214	0.61	0.81	29	empty
3	238	0.60	0.80	34	empty
4	277	0.57	0.78	39	empty
5	310	0.56	0.76	50	empty

Interfaces

1 interface between chains.

B–A · 156 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5XGQ · Crystal structure of apo form (free-state) Mycobacterium tuberculosis methionyl-tRNA… · the same entry in another collection · chain B against B, 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 A5U150
Elsewhere: RCSB PDB 5XGQ · PDBe 5XGQ · UniProt A5U150

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