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Crystal structure of translation elongation factor ef-1 beta from pyrococcus horikoshii

Analyse Crystal structure of translation elongation factor ef-1 beta from pyrococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YY3
Type
protein
Length
273 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Elongation factor 1-beta
UniProt
P58748
Pockets
3 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CElongation factor 1-betaprotein9123% helix, 42% strandP58748

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11660.470.7632empty
21040.450.7918empty
3500.330.7814empty

Interfaces

2 interfaces between chains.

  • A–B · 540 Ų buried · 9 hydrogen bonds · protein-protein
  • A–C · 197 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 2YY3 · Crystal Structure of translation elongation factor EF-1 beta from Pyrococcus horikoshii · the same entry in another collection · chain A against A, TM-score 1.00
  • P58748 · AlphaFold monomer V2.0 prediction for elongation factor 1-beta (P58748) · a predicted model of the same protein · chain C against A, TM-score 0.97

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