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Crystal structure of ttnrs

Analyse Crystal structure of ttnrs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZG8
Type: protein
Length: 422 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Asparagine--tRNA ligase
EC: 6.1.1.22
UniProt: P54263
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Asparagine--tRNA ligase (EC 6.1.1.22)	protein	422	37% helix, 29% strand	P54263

Pockets

3 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	570	0.65	0.76	61	empty
2	129	0.53	0.81	19	empty
3	67	0.32	0.75	18	empty

Compared structures

5ZG8 · Crystal Structure of TtNRS · the same entry in another collection · chain A against A, TM-score 1.00
P54263 · AlphaFold monomer V2.0 prediction for asparagine--tRNA ligase (P54263) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P54263
Elsewhere: RCSB PDB 5ZG8 · PDBe 5ZG8 · UniProt P54263

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