PDBe 1m5y

X-ray diffraction
3Å resolution

Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone SurA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 408 amino acids
Theoretical weight: 45.13 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0ABZ6 (Residues: 21-428; Coverage: 100%)
Gene names: JW0052, b0053, surA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: F222
Unit cell:
a: 158.817Å b: 223.406Å c: 279.721Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.228 0.283
Expression system: Escherichia coli BL21(DE3)