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Crystal structure of elongation factor 2 GDP-form

Analyse Crystal structure of elongation factor 2 GDP-form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5H7K
Type
protein
Length
367 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Elongation factor 2
UniProt
O59521
Ligands
GDP
Pockets
2 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AElongation factor 2protein36736% helix, 26% strandO59521

Ligands and binding sites

  • GDP · Guanosine-5'-diphosphate · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11100.600.8634empty
2540.350.7915empty

Compared structures

  • 5H7K · Crystal structure of Elongation factor 2 GDP-form · the same entry in another collection · chain A against A, TM-score 1.00
  • O59521 · AlphaFold monomer V2.0 prediction for elongation factor 2 (O59521) · a predicted model of the same protein · chain A against A, TM-score 0.96

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