› 2hst

Solution NMR

Solution structure of the middle domain of human eukaryotic translation termination factor eRF1

Released:
DOI: 10.2210/pdb2hst/pdb
PDB entry 2hst coloured by chain, ensemble of 25 models, front view.
PDB entry 2hst coloured by chain, ensemble of 25 models, side view.
PDB entry 2hst coloured by chain, ensemble of 25 models, top view.
Source organism: Homo sapiens
Primary publication:
Eukaryotic class 1 translation termination factor eRF1--the NMR structure and dynamics of the middle domain involved in triggering ribosome-dependent peptidyl-tRNA hydrolysis.
Ivanova EV, Kolosov PM, Birdsall B, Kelly G, Pastore A, Kisselev LL, Polshakov VI
FEBS J 274 4223-37 (2007)
PMID: 17651434

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-158631 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Eukaryotic peptide chain release factor subunit 1 Chain: A
Molecule details ›
Chain: A
Length: 143 amino acids
Theoretical weight: 15.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P62495 (Residues: 140-275; Coverage: 31%)
Gene names: ERF1, ETF1, RF1, SUP45L1
Sequence domains: eRF1 domain 2
Structure domains: eRF1 domain 2

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

1 review citation

Peptide release on the ribosome: mechanism and implications for translational control.
Youngman et al. (2008)
8 other articles

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)