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Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA asp

Analyse Class II aminoacyl transfer RNA synthetases: crystal structure of yeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ASY
Type
protein + RNA
Length
1,130 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
T-RNA (75-mer); Aspartyl-tRNA synthetase
EC
6.1.1.12
UniProt
P04802
Pockets
17 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
R, ST-RNA (75-mer) (EC 6.1.1.12)rna75——
A, BAspartyl-tRNA synthetaseprotein49030% helix, 23% strandP04802

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17910.850.8880empty
25150.820.8883empty
310790.800.8274empty
411490.790.8170empty
58600.750.8048empty

Interfaces

4 interfaces between chains.

  • A–B · 4751 Ų buried · 80 hydrogen bonds · protein-protein
  • R–A · 2284 Ų buried · 57 hydrogen bonds · protein-nucleic
  • S–B · 2161 Ų buried · 63 hydrogen bonds · protein-nucleic
  • S–A · 24 Ų buried · 0 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 16 modified (nucleotide modification).

Compared structures

  • 1ASY · Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA… · the same entry in another collection · chain R against R, TM-score 1.00
  • P04802 · AlphaFold monomer V2.0 prediction for aspartate--tRNA ligase, cytoplasmic (P04802) · a predicted model of the same protein · chain A against A, TM-score 0.98

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