1h2i

X-ray diffraction
2.7Å resolution

Human Rad52 protein, N-terminal domain

Released:
Source organism: Homo sapiens
Primary publication:
Structure of the single-strand annealing domain of human RAD52 protein.
Proc Natl Acad Sci U S A 99 13492-7 (2002)
PMID: 12370410

Function and Biology Details

Structure analysis Details

Assembly composition:
homo undecamer (preferred)
PDBe Complex ID:
PDB-CPX-155038 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA repair protein RAD52 homolog Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V
Length: 209 amino acids
Theoretical weight: 23.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P43351 (Residues: 1-209; Coverage: 50%)
Gene name: RAD52
Sequence domains: Rad52/22 family double-strand break repair protein
Structure domains: DNA repair protein Rad52/59/22

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21
Unit cell:
a: 117.259Å b: 127.319Å c: 191.227Å
α: 90° β: 90.29° γ: 90°
R-values:
R R work R free
0.225 0.225 0.262
Expression system: Escherichia coli