› 5izk

X-ray diffraction
3.25Å resolution

The crystal structure of human eEFSec in complex with GDP

Released:
DOI: 10.2210/pdb5izk/pdb
PDB entry 5izk coloured by chain, front view.
PDB entry 5izk coloured by chain, side view.
PDB entry 5izk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation.
Dobosz-Bartoszek M, Pinkerton MH, Otwinowski Z, Chakravarthy S, Söll D, Copeland PR, Simonović M
Nat Commun 7 12941 (2016)
PMID: 27708257

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-157636 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Selenocysteine-specific elongation factor Chains: A, B
Molecule details ›
Chains: A, B
Length: 616 amino acids
Theoretical weight: 67.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P57772 (Residues: 1-596; Coverage: 100%)
Gene names: EEFSEC, SELB
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand GDP 2 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 58.691Å b: 96.861Å c: 125.408Å
α: 90° β: 90.25° γ: 90°
R-values:
R R work R free
0.298 0.296 0.338
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The unique tRNASec and its role in selenocysteine biosynthesis.
Serrão et al. (2018)
2 more

2 mentions without citation

Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation.
Dobosz-Bartoszek et al. (2016)
1 more