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Crystal structure of a mutant elongation factor G trapped with a GTP analogue

Analyse Crystal structure of a mutant elongation factor G trapped with a GTP analogue in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2BV3
Type
protein
Length
632 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Elongation factor G
UniProt
P13551
Ligands
GNP, MG
Pockets
9 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AElongation factor Gprotein63226% helix, 34% strandP13551

Ligands and binding sites

  • GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
  • MG · Magnesium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16320.700.7862empty
24650.700.8169empty
3650.650.9317empty
41520.540.8024empty
5510.370.8019empty

Compared structures

  • 2BV3 · Crystal structure of a mutant elongation factor G trapped with a GTP analogue · the same entry in another collection · chain A against A, TM-score 1.00
  • P13551 · AlphaFold monomer V2.0 prediction for elongation factor G (P13551) · a predicted model of the same protein · chain A against A, TM-score 0.77

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