› 2mvn

Solution NMR

Solution structure of eEF1Bdelta CAR domain in TCTP-bound state

Released:
DOI: 10.2210/pdb2mvn/pdb
PDB entry 2mvn coloured by chain, ensemble of 20 models, front view.
PDB entry 2mvn coloured by chain, ensemble of 20 models, side view.
PDB entry 2mvn coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Evolutionarily conserved binding of translationally controlled tumor protein to eukaryotic elongation factor 1B.
Wu H, Gong W, Yao X, Wang J, Perrett S, Feng Y
J Biol Chem 290 8694-710 (2015)
PMID: 25635048

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151562 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Elongation factor 1-delta Chain: A
Molecule details ›
Chain: A
Length: 44 amino acids
Theoretical weight: 5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29692 (Residues: 153-192; Coverage: 14%)
Gene names: EEF1D, EF1D
Sequence domains: Eukaryotic elongation factor 1 beta central acidic region

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 74%
Refinement method: molecular dynamics simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Dysregulation of TCTP in Biological Processes and Diseases.
Bommer et al. (2020)
1 more

1 mention without citation

Evolutionarily conserved binding of translationally controlled tumor protein to eukaryotic elongation factor 1B.
Wu et al. (2015)