› 3pvs

X-ray diffraction
2.5Å resolution

Structure and biochemical activities of Escherichia coli MgsA

Released:
DOI: 10.2210/pdb3pvs/pdb
Model geometry
Fit model/data
PDB entry 3pvs coloured by chain, front view.
PDB entry 3pvs coloured by chain, side view.
PDB entry 3pvs coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure and biochemical activities of Escherichia coli MgsA.
Page AN, George NP, Marceau AH, Cox MM, Keck JL
J Biol Chem 286 12075-85 (2011)
PMID: 21297161

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163898 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Replication-associated recombination protein A Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 447 amino acids
Theoretical weight: 49.69 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 99.946Å b: 143.689Å c: 163.186Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.195 0.266
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Generation and Repair of Postreplication Gaps in Escherichia coli.
Cox et al. (2023)
19 other articles

1 mention without citation

Structure and biochemical activities of Escherichia coli MgsA.
Page et al. (2011)