PDBe 2pv2

X-ray diffraction
1.3Å resolution

Crystallographic Structure of SurA first peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRK


Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0). 
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
C-peptide Chains: E, F
Molecule details ›
Chains: E, F
Length: 12 amino acids
Theoretical weight: 1.62 KDa
Source organism: Synthetic construct
Expression system: Not provided
Chaperone SurA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 103 amino acids
Theoretical weight: 10.98 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P0ABZ6 (Residues: 172-274; Coverage: 25%)
Gene names: JW0052, b0053, surA
Sequence domains: PPIC-type PPIASE domain
Structure domains: Chitinase A; domain 3

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P21
Unit cell:
a: 56.46Å b: 50.63Å c: 74.06Å
α: 90° β: 111.54° γ: 90°
R R work R free
0.208 0.208 0.227
Expression systems:
  • Not provided
  • Escherichia coli BL21(DE3)