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Crystal structure of apo tias (TRNAILE2 agmatidine synthetase)

Analyse Crystal structure of apo tias (TRNAILE2 agmatidine synthetase) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5XOB
Type
protein
Length
417 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TRNA(ILE2) 2-agmatinylcytidine synthetase tias
EC
6.3.4.22
UniProt
O28025
Ligands
ZN, MG
Pockets
3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ZTRNA(ILE2) 2-agmatinylcytidine synthetase tias (EC 6.3.4.22)protein41726% helix, 32% strandO28025

Ligands and binding sites

  • ZN · Zinc ion · metal · chains Z
  • MG · Magnesium ion · metal · chains Z

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16670.720.7966MG
21190.680.9027empty
3650.360.7813empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 5XOB · Crystal structure of apo TiaS (tRNAIle2 agmatidine synthetase) · the same entry in another collection · chain Z against Z, TM-score 1.00
  • O28025 · AlphaFold monomer V2.0 prediction for TRNA(ILE2) 2-agmatinylcytidine synthetase tias… · a predicted model of the same protein · chain Z against A, TM-score 0.97

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