› 1pbu

Solution NMR

Solution structure of the C-terminal domain of the human eEF1Bgamma subunit

Released:
DOI: 10.2210/pdb1pbu/pdb
PDB entry 1pbu coloured by chain, ensemble of 20 models, front view.
PDB entry 1pbu coloured by chain, ensemble of 20 models, side view.
PDB entry 1pbu coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
1H, 15N and 13C resonance assignments of the highly conserved 19 kDa C-terminal domain from human elongation factor 1Bgamma.
Vanwetswinkel S, Kriek J, Andersen GR, Dijk J, Siegal G
J Biomol NMR 26 189-90 (2003)
PMID: 12766415

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150789 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Elongation factor 1-gamma Chain: A
Molecule details ›
Chain: A
Length: 162 amino acids
Theoretical weight: 19.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P26641 (Residues: 276-437; Coverage: 37%)
Gene names: EEF1G, EF1G, PRO1608
Sequence domains: Elongation factor 1 gamma, conserved domain
Structure domains: Translation elongation factor EF1B, gamma chain, conserved domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics, simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

Purification and characterisation of recombinant human eukaryotic elongation factor 1 gamma.
Achilonu et al. (2014)
2 more

3 mentions without citation

Detecting remotely related proteins by their interactions and sequence similarity.
Espadaler et al. (2005)
2 more