4ern

X-ray diffraction
1.8Å resolution

Crystal structure of the C-terminal domain of human XPB/ERCC-3 excision repair protein at 1.80 A

Released:
Source organism: Homo sapiens
Primary publication:
Structure of the C-terminal half of human XPB helicase and the impact of the disease-causing mutation XP11BE.
Acta Crystallogr D Biol Crystallogr 69 237-46 (2013)
PMID: 23385459

Function and Biology Details

Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-148581 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
General transcription and DNA repair factor IIH helicase/translocase subunit XPB Chain: A
Molecule details ›
Chain: A
Length: 289 amino acids
Theoretical weight: 33.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P19447 (Residues: 494-782; Coverage: 37%)
Gene names: ERCC3, XPB, XPBC
Sequence domains: ERCC3/RAD25/XPB C-terminal helicase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 38.26Å b: 73.65Å c: 84.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.201 0.238
Expression system: Escherichia coli