PDBe 2pv3

X-ray diffraction
3.39Å resolution

Crystallographic Structure of SurA fragment lacking the second peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRK

Released:

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 Chain: C
Molecule details ›
Chain: C
Length: 12 amino acids
Theoretical weight: 1.62 KDa
Source organism: Synthetic construct
Expression system: Not provided
UniProt:
Chaperone SurA Chains: A, B
Molecule details ›
Chains: A, B
Length: 299 amino acids
Theoretical weight: 33.22 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0ABZ6 (Residues: 21-428; Coverage: 73%)
Gene names: JW0052, b0053, surA
Sequence domains:
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: P3221
Unit cell:
a: 148.33Å b: 148.33Å c: 188.68Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.284 0.284 0.299
Expression systems:
  • Not provided
  • Escherichia coli BL21(DE3)