› 1b64

Solution NMR

SOLUTION STRUCTURE OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR DOMAIN FROM HUMAN ELONGATION FACTOR-ONE BETA, NMR, 20 STRUCTURES

Released:
DOI: 10.2210/pdb1b64/pdb
PDB entry 1b64 coloured by chain, ensemble of 20 models, front view.
PDB entry 1b64 coloured by chain, ensemble of 20 models, side view.
PDB entry 1b64 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli.
Pérez JM, Siegal G, Kriek J, Hård K, Dijk J, Canters GW, Möller W
Structure 7 217-26 (1999)
PMID: 10368288

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150244 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Elongation factor 1-beta Chain: A
Molecule details ›
Chain: A
Length: 91 amino acids
Theoretical weight: 10.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P24534 (Residues: 136-225; Coverage: 40%)
Gene names: EEF1B, EEF1B2, EF1B
Sequence domains: EF-1 guanine nucleotide exchange domain
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

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

Quick links

Citations

5 review citations

Elongation factors in protein biosynthesis.
Andersen et al. (2003)
4 more

8 mentions without citation

Chemical shift prediction for protein structure calculation and quality assessment using an optimally parameterized force field.
Nielsen et al. (2012)
7 more