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Crystal structure of the archaeal asparagine synthetase a

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

PDB
3P8T
Type
protein
Length
588 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Asns-like asparaginyl-tRNA synthetase related protein
UniProt
Q9V228
Pockets
6 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAsns-like asparaginyl-tRNA synthetase related proteinprotein29437% helix, 23% strandQ9V228

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12730.800.9253empty
22850.790.9153empty
3840.390.7817empty
4680.340.7615empty
5770.340.7519empty

Interfaces

1 interface between chains.

  • A–B · 2955 Ų buried · 28 hydrogen bonds · protein-protein

Compared structures

  • 3P8T · Crystal structure of the archaeal asparagine synthetase A · the same entry in another collection · chain A against A, TM-score 1.00

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