5u6k

X-ray diffraction
2.6Å resolution

Crystal structure of TopBP1 BRCT4/5 in complex with a BLM phosphopeptide

Released:
Source organisms:
Primary publication:
Structural Insight into BLM Recognition by TopBP1.
Structure 25 1582-1588.e3 (2017)
PMID: 28919440

Function and Biology Details

Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-156945 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA topoisomerase 2-binding protein 1 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 200 amino acids
Theoretical weight: 21.69 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6ZQF0 (Residues: 553-746; Coverage: 13%)
Gene names: Kiaa0259, Topbp1
Sequence domains: twin BRCT domain
Structure domains: BRCT domain
RecQ-like DNA helicase BLM Chains: L, M, N, O
Molecule details ›
Chains: L, M, N, O
Length: 13 amino acids
Theoretical weight: 1.54 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P54132 (Residues: 297-309; Coverage: 1%)
Gene names: BLM, RECQ2, RECQL3

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P21
Unit cell:
a: 98.164Å b: 96.817Å c: 127.05Å
α: 90° β: 94.25° γ: 90°
R-values:
R R work R free
0.221 0.219 0.256
Expression systems:
  • Escherichia coli
  • Not provided