5cqr

X-ray diffraction
3.02Å resolution

Dimerization of Elp1 is essential for Elongator complex assembly

Released:
Source organism: Homo sapiens
Primary publication:
Dimerization of elongator protein 1 is essential for Elongator complex assembly.
Proc. Natl. Acad. Sci. U.S.A. 112 10697-702 (2015)
PMID: 26261306

Function and Biology Details

Biochemical function:
  • not assigned
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Elongator complex protein 1 Chain: A
Molecule details ›
Chain: A
Length: 622 amino acids
Theoretical weight: 71.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95163 (Residues: 715-1332; Coverage: 46%)
Gene names: ELP1, IKAP, IKBKAP

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P6122
Unit cell:
a: 73.02Å b: 73.02Å c: 479.508Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.221 0.27
Expression system: Escherichia coli