› 2a1i

X-ray diffraction
1.9Å resolution

Crystal Structure of the Central Domain of Human ERCC1

Released:
DOI: 10.2210/pdb2a1i/pdb
PDB entry 2a1i coloured by chain, front view.
PDB entry 2a1i coloured by chain, side view.
PDB entry 2a1i coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure and DNA binding functions of ERCC1, a subunit of the DNA structure-specific endonuclease XPF-ERCC1.
Tsodikov OV, Enzlin JH, Schärer OD, Ellenberger T
Proc Natl Acad Sci U S A 102 11236-41 (2005)
PMID: 16076955

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139873 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA excision repair protein ERCC-1 Chain: A
Molecule details ›
Chain: A
Length: 146 amino acids
Theoretical weight: 16.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07992 (Residues: 96-227; Coverage: 44%)
Gene name: ERCC1
Sequence domains: Binding domain of DNA repair protein Ercc1 (rad10/Swi10)
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand HG 1 x HG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 40.07Å b: 50.291Å c: 72.216Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.204 0.248
Expression system: Escherichia coli

Quick links

Citations

28 review citations

Structural and functional relationships of the XPF/MUS81 family of proteins.
Ciccia et al. (2008)
27 more

13 mentions without citation

DNA repair endonuclease ERCC1-XPF as a novel therapeutic target to overcome chemoresistance in cancer therapy.
McNeil et al. (2012)
12 more