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X-ray diffraction
1.8Å resolution

Crystal structure of RPA70N-BLMp2 fusion

Released:

Function and Biology Details

Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-218079 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RecQ-like DNA helicase BLM; Replication protein A 70 kDa DNA-binding subunit, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 146 amino acids
Theoretical weight: 16.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P27694 (Residues: 1-121; Coverage: 20%)
  • Canonical: P54132 (Residues: 550-570; Coverage: 2%)
Gene names: BLM, RECQ2, RECQL3, REPA1, RPA1, RPA70
Sequence domains: Replication factor-A protein 1, N-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: P41212
Unit cell:
a: 62.476Å b: 62.476Å c: 69.497Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.193 0.217
Expression system: Escherichia coli