› 4ipd

X-ray diffraction
1.51Å resolution

Structure of the N-terminal domain of RPA70, E100R mutant

Released:
DOI: 10.2210/pdb4ipd/pdb
PDB entry 4ipd coloured by chain, front view.
PDB entry 4ipd coloured by chain, side view.
PDB entry 4ipd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Surface reengineering of RPA70N enables cocrystallization with an inhibitor of the replication protein A interaction motif of ATR interacting protein.
Feldkamp MD, Frank AO, Kennedy JP, Patrone JD, Vangamudi B, Waterson AG, Fesik SW, Chazin WJ
Biochemistry 52 6515-24 (2013)
PMID: 23962067

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151049 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Replication protein A 70 kDa DNA-binding subunit, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 123 amino acids
Theoretical weight: 13.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P27694 (Residues: 1-120; Coverage: 20%)
Gene names: REPA1, RPA1, RPA70
Sequence domains: Replication factor-A protein 1, N-terminal domain
Structure domains: Nucleic acid-binding proteins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 39.425Å b: 50.149Å c: 51.867Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.138 0.136 0.166
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Interactive Roles of DNA Helicases and Translocases with the Single-Stranded DNA Binding Protein RPA in Nucleic Acid Metabolism.
Awate et al. (2017)
2 more

1 mention without citation

Surface reengineering of RPA70N enables cocrystallization with an inhibitor of the replication protein A interaction motif of ATR interacting protein.
Feldkamp et al. (2013)