X-ray diffraction
2.55Å resolution

2.55 Angstrom Resolution Crystal Structure of Peptidylprolyl Isomerase (PrsA) from Bacillus cereus

Source organism: Bacillus cereus ATCC 14579
Entry authors: Minasov G, Shuvalova L, Dubrovska I, Kiryukhina O, Wiersum G, Endres M, Satchell KJF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Foldase protein PrsA 4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 258 amino acids
Theoretical weight: 30.01 KDa
Source organism: Bacillus cereus ATCC 14579
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q81CB1 (Residues: 26-280; Coverage: 99%)
Gene names: BC_2862, prsA4
Sequence domains: PPIC-type PPIASE domain

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: C2
Unit cell:
a: 151.425Å b: 70.358Å c: 79.357Å
α: 90° β: 91.749° γ: 90°
R R work R free
0.219 0.217 0.247
Expression system: Escherichia coli BL21(DE3)