Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139875 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA excision repair protein ERCC-1
Molecule details ›
Chain: A
Length: 96 amino acids
Theoretical weight: 10.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Helix-hairpin-helix motif
Structure domains: 5' to 3' exonuclease, C-terminal subdomain
Length: 96 amino acids
Theoretical weight: 10.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
P07992 (Residues: 220-297; Coverage: 26%)
Sequence domains: Helix-hairpin-helix motif
Structure domains: 5' to 3' exonuclease, C-terminal subdomain
DNA repair endonuclease XPF
Molecule details ›
Chain: B
Length: 84 amino acids
Theoretical weight: 9.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Structure domains: 5' to 3' exonuclease, C-terminal subdomain
Length: 84 amino acids
Theoretical weight: 9.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical: Q92889 (Residues: 834-916; Coverage: 9%)
Structure domains: 5' to 3' exonuclease, C-terminal subdomain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
89%
Refinement method:
restrained molecular dynamics
Expression system: Escherichia coli BL21
