MolNFT v1 · #75363 · protein

Structure of glutamyl-tRNA synthetase from mycobacterium tuberculosis in space group P21

3PNY: “Structure of glutamyl-tRNA synthetase from mycobacterium tuberculosis in space group P21”. X-ray diffraction, 10 pockets (best druggability 0.70). MolNFT v1 #75363 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3PNY
Type: protein
Length: 966 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamyl-tRNA synthetase
EC: 6.1.1.17
UniProt: P0A636
Pockets: 10 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamyl-tRNA synthetase (EC 6.1.1.17)	protein	481	51% helix, 11% strand	P0A636
B	Glutamyl-tRNA synthetase (EC 6.1.1.17)	protein	485	49% helix, 12% strand	P0A636

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	526	0.70	0.80	50	empty
2	455	0.67	0.79	42	empty
3	412	0.59	0.75	33	empty
4	406	0.58	0.75	29	empty
5	125	0.55	0.83	27	empty

Interfaces

1 interface between chains.

A–B · 844 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

3PNY · Structure of Glutamyl-tRNA synthetase from Mycobacterium tuberculosis in space group P21 · the same entry in another collection · chain A against A, 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 P0A636
Elsewhere: RCSB PDB 3PNY · PDBe 3PNY · UniProt P0A636

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