› 1quq

X-ray diffraction
2.5Å resolution

COMPLEX OF REPLICATION PROTEIN A SUBUNITS RPA14 AND RPA32

Released:
DOI: 10.2210/pdb1quq/pdb
PDB entry 1quq coloured by chain, front view.
PDB entry 1quq coloured by chain, side view.
PDB entry 1quq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding.
Bochkarev A, Bochkareva E, Frappier L, Edwards AM
EMBO J 18 4498-504 (1999)
PMID: 10449415

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147543 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Replication protein A 32 kDa subunit Chains: A, C
Molecule details ›
Chains: A, C
Length: 129 amino acids
Theoretical weight: 14.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15927 (Residues: 43-171; Coverage: 48%)
Gene names: REPA2, RPA2, RPA32, RPA34
Structure domains: Nucleic acid-binding proteins
Replication protein A 14 kDa subunit Chains: B, D
Molecule details ›
Chains: B, D
Length: 121 amino acids
Theoretical weight: 13.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35244 (Residues: 1-121; Coverage: 100%)
Gene names: REPA3, RPA14, RPA3
Sequence domains: Replication factor A protein 3
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: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 65.7Å b: 76.6Å c: 119.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.291
Expression system: Escherichia coli

Quick links

Citations

26 review citations

Nucleic acid recognition by OB-fold proteins.
Theobald et al. (2003)
25 more

10 mentions without citation

Structural biology of telomeres and telomerase.
Smith et al. (2020)
9 more