› 3g65

X-ray diffraction
2.9Å resolution

Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex

Released:
DOI: 10.2210/pdb3g65/pdb
PDB entry 3g65 coloured by chain, front view.
PDB entry 3g65 coloured by chain, side view.
PDB entry 3g65 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the rad9-rad1-hus1 DNA damage checkpoint complex--implications for clamp loading and regulation.
Doré AS, Kilkenny ML, Rzechorzek NJ, Pearl LH
Mol Cell 34 735-45 (2009)
PMID: 19446481

Function and Biology Details

Reaction catalysed: 
Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130056 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Cell cycle checkpoint control protein RAD9A Chain: A
Molecule details ›
Chain: A
Length: 296 amino acids
Theoretical weight: 32.45 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q99638 (Residues: 1-270; Coverage: 69%)
Gene name: RAD9A
Sequence domains: Rad9
Structure domains: Proliferating Cell Nuclear Antigen
Cell cycle checkpoint protein RAD1 Chain: B
Molecule details ›
Chain: B
Length: 282 amino acids
Theoretical weight: 31.85 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O60671 (Residues: 1-282; Coverage: 100%)
Gene names: RAD1, REC1
Sequence domains: Repair protein Rad1/Rec1/Rad17
Structure domains: Proliferating Cell Nuclear Antigen
Checkpoint protein HUS1 Chain: C
Molecule details ›
Chain: C
Length: 280 amino acids
Theoretical weight: 31.73 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O60921 (Residues: 1-280; Coverage: 100%)
Gene name: HUS1
Sequence domains: Hus1-like protein
Structure domains: Proliferating Cell Nuclear Antigen

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1, ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 73.246Å b: 70.673Å c: 83.151Å
α: 90° β: 99.51° γ: 90°
R-values:
R R work R free
0.224 0.221 0.272
Expression system: Spodoptera frugiperda

Quick links

Citations

9 review citations

Functional interplay between ATM/ATR-mediated DNA damage response and DNA repair pathways in oxidative stress.
Yan et al. (2014)
8 more

11 mentions without citation

MultiBac: expanding the research toolbox for multiprotein complexes.
Bieniossek et al. (2012)
10 more