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Crystal structure of eukaryotic translation initiation factor eif-5A2 from arabidopsis thaliana

Analyse Crystal structure of eukaryotic translation initiation factor eif-5A2 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3HKS
Type
protein
Length
286 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Eukaryotic translation initiation factor 5A-2
UniProt
Q93VP3
Pockets
3 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 55% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEukaryotic translation initiation factor 5A-2protein14410% helix, 56% strandQ93VP3
BEukaryotic translation initiation factor 5A-2protein14211% helix, 55% strandQ93VP3

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 6 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1970.380.7618empty
2890.300.7312empty
3700.280.7216EDO

Interfaces

1 interface between chains.

  • A–B · 484 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 3HKS · Crystal structure of eukaryotic translation initiation factor eIF-5A2 from Arabidopsis… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q93VP3 · AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 5A-2… · a predicted model of the same protein · chain B against A, TM-score 0.92

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