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Crystal structure of ribosomal elongation factor (ef)-G from staphylococcus aureus with a fusidic acid hyper-sensitivity mutation M16I

Analyse Crystal structure of ribosomal elongation factor (ef)-G from staphylococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ZZ0
Type
protein
Length
1,296 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Elongation factor G
UniProt
P68790
Pockets
17 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BElongation factor Gprotein64831% helix, 33% strandP68790

Pockets

17 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19830.780.8093empty
26480.740.8070empty
31110.590.8528empty
41290.580.8419empty
5950.570.8518empty

Interfaces

1 interface between chains.

  • A–B · 361 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 3ZZ0 · Crystal structure of ribosomal elongation factor (EF)-G from Staphylococcus aureus with a… · the same entry in another collection · chain A against A, TM-score 1.00
  • P68790 · AlphaFold monomer V2.0 prediction for elongation factor G (P68790) · a predicted model of the same protein · chain B against A, TM-score 0.75

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