› 1b22

Solution NMR

RAD51 (N-TERMINAL DOMAIN)

Released:
DOI: 10.2210/pdb1b22/pdb
PDB entry 1b22 coloured by chain, ensemble of 30 models, front view.
PDB entry 1b22 coloured by chain, ensemble of 30 models, side view.
PDB entry 1b22 coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR.
Aihara H, Ito Y, Kurumizaka H, Yokoyama S, Shibata T
J Mol Biol 290 495-504 (1999)
PMID: 10390347

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170369 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA repair protein RAD51 homolog 1 Chain: A
Molecule details ›
Chain: A
Length: 114 amino acids
Theoretical weight: 12.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q06609 (Residues: 1-114; Coverage: 34%)
Gene names: RAD51, RAD51A, RECA
Sequence domains: Helix-hairpin-helix domain
Structure domains: 5' to 3' exonuclease, C-terminal subdomain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: RANDOM SIMULATED ANNEALING
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Role of RAD52 epistasis group genes in homologous recombination and double-strand break repair.
Symington LS. (2002)
14 more

14 mentions without citation

Fanconi anemia pathway as a prospective target for cancer intervention.
Liu et al. (2020)
13 more