› 1xpa

Solution NMR

SOLUTION STRUCTURE OF THE DNA-AND RPA-BINDING DOMAIN OF THE HUMAN REPAIR FACTOR XPA, NMR, 1 STRUCTURE

Released:
DOI: 10.2210/pdb1xpa/pdb
PDB entry 1xpa coloured by chain, front view.
PDB entry 1xpa coloured by chain, side view.
PDB entry 1xpa coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA.
Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M
Nat Struct Biol 5 701-6 (1998)
PMID: 9699634

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149868 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA repair protein complementing XP-A cells Chain: A
Molecule details ›
Chain: A
Length: 122 amino acids
Theoretical weight: 14.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P23025 (Residues: 98-219; Coverage: 45%)
Gene names: XPA, XPAC
Sequence domains:
Structure domains: XPA C-terminal domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry
Expression system: Escherichia coli BL21

Quick links

Citations

15 review citations

Flexible nets. The roles of intrinsic disorder in protein interaction networks.
Dunker et al. (2005)
14 more

22 mentions without citation

XPA: A key scaffold for human nucleotide excision repair.
Sugitani et al. (2016)
21 more