MolNFT v1 · #15604 · protein

Crystal structure of the non-discriminating and archaeal- type aspartyl-tRNA synthetase from thermus thermophilus

1N9W · Aspartyl-tRNA synthetase 2: “Crystal structure of the non-discriminating and archaeal- type aspartyl-tRNA synthetase from thermus…”. X-ray diffraction, 7 pockets (best druggability 0.61). MolNFT v1 #15604 on GenesisL1: 3D structure…

PDB: 1N9W
Type: protein
Length: 715 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aspartyl-tRNA synthetase 2
UniProt: Q9LCY8
Pockets: 7 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aspartyl-tRNA synthetase 2	protein	356	38% helix, 29% strand	Q9LCY8
B	Aspartyl-tRNA synthetase 2	protein	359	36% helix, 29% strand	Q9LCY8

Pockets

7 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	236	0.61	0.81	43	empty
2	222	0.56	0.78	51	empty
3	183	0.47	0.76	36	empty
4	69	0.38	0.78	20	empty
5	60	0.29	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 3051 Å² buried · 46 hydrogen bonds · protein-protein

Compared structures

1N9W · Crystal structure of the non-discriminating and archaeal-type aspartyl-tRNA synthetase… · 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 Q9LCY8
Elsewhere: RCSB PDB 1N9W · PDBe 1N9W · UniProt Q9LCY8

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