3ggr

X-ray diffraction
3.2Å resolution

Crystal Structure of the Human Rad9-Hus1-Rad1 complex

Released:
Source organism: Homo sapiens

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:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Cell cycle checkpoint control protein RAD9A Chain: A
Molecule details ›
Chain: A
Length: 270 amino acids
Theoretical weight: 29.75 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q99638 (Residues: 1-270; Coverage: 69%)
Gene name: RAD9A
Sequence domains: Rad9
Structure domains: Proliferating Cell Nuclear Antigen
Checkpoint protein HUS1 Chain: B
Molecule details ›
Chain: B
Length: 286 amino acids
Theoretical weight: 32.56 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: O60921 (Residues: 2-280; Coverage: 100%)
  • Best match: O60921-2 (Residues: 1-259)
Gene name: HUS1
Structure domains: Proliferating Cell Nuclear Antigen
Cell cycle checkpoint protein RAD1 Chain: C
Molecule details ›
Chain: C
Length: 282 amino acids
Theoretical weight: 31.85 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
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

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU, SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 71.029Å b: 67.164Å c: 83.405Å
α: 90° β: 97.58° γ: 90°
R-values:
R R work R free
0.291 0.289 0.306
Expression system: Komagataella pastoris