› 3a1j

X-ray diffraction
2.5Å resolution

Crystal structure of the human Rad9-Hus1-Rad1 complex

Released:
DOI: 10.2210/pdb3a1j/pdb
PDB entry 3a1j coloured by chain, front view.
PDB entry 3a1j coloured by chain, side view.
PDB entry 3a1j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the human rad9-hus1-rad1 clamp.
Sohn SY, Cho Y
J Mol Biol 390 490-502 (2009)
PMID: 19464297

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 (4 distinct):
Cell cycle checkpoint control protein RAD9A Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 29.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99638 (Residues: 1-266; Coverage: 68%)
Gene name: RAD9A
Sequence domains: Rad9
Structure domains: Proliferating Cell Nuclear Antigen
Checkpoint protein HUS1 Chain: B
Molecule details ›
Chain: B
Length: 281 amino acids
Theoretical weight: 32.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60921 (Residues: 1-280; Coverage: 100%)
Gene name: HUS1
Sequence domains: Hus1-like protein
Structure domains: Proliferating Cell Nuclear Antigen
Cell cycle checkpoint protein RAD1 Chain: C
Molecule details ›
Chain: C
Length: 263 amino acids
Theoretical weight: 30.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60671 (Residues: 13-275; Coverage: 93%)
Gene names: RAD1, REC1
Sequence domains: Repair protein Rad1/Rec1/Rad17
Structure domains: Proliferating Cell Nuclear Antigen

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
No bound ligands
1 modified residue:
Ligand MSE 22 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P21
Unit cell:
a: 77.154Å b: 70.776Å c: 86.661Å
α: 90° β: 99.2° γ: 90°
R-values:
R R work R free
0.209 0.209 0.282
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Eukaryotic DNA damage checkpoint activation in response to double-strand breaks.
Finn et al. (2012)
5 more

7 mentions without citation

Association of the Rad9-Rad1-Hus1 checkpoint clamp with MYH DNA glycosylase and DNA.
Hwang et al. (2015)
6 more