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Crystal structure of alanyl-tRNA synthetase from pyrococcus horikoshii OT3

Analyse Crystal structure of alanyl-tRNA synthetase from pyrococcus horikoshii OT3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1V4P
Type
protein
Length
457 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alanyl-tRNA synthetase
EC
6.1.1.7
UniProt
O58307
Ligands
ZN
Pockets
7 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAlanyl-tRNA synthetase (EC 6.1.1.7)protein15136% helix, 33% strandO58307
CAlanyl-tRNA synthetase (EC 6.1.1.7)protein15536% helix, 32% strandO58307

Ligands and binding sites

  • ZN · Zinc ion · metal · 3 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13510.660.8034empty
22600.620.8038empty
32680.600.7923empty
42390.580.7935empty
51620.490.7727empty

Interfaces

3 interfaces between chains.

  • A–C · 607 Ų buried · 9 hydrogen bonds · protein-protein
  • B–C · 535 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 18 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1V4P · Crystal structure of Alanyl-tRNA Synthetase from Pyrococcus horikoshii OT3 · the same entry in another collection · chain A against A, TM-score 1.00
  • O58307 · AlphaFold monomer V2.0 prediction for alanyl-tRNA editing protein alax-S (O58307) · a predicted model of the same protein · chain B against A, TM-score 0.99

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