› 3b09

X-ray diffraction
1.9Å resolution

Crystal structure of the N-domain of FKBP22 from Shewanella sp. SIB1

Released:
DOI: 10.2210/pdb3b09/pdb
PDB entry 3b09 coloured by chain, front view.
PDB entry 3b09 coloured by chain, side view.
PDB entry 3b09 coloured by chain, top view.
Source organism: Shewanella sp. SIB1
Primary publication:
Crystal structure of N-domain of FKBP22 from Shewanella sp. SIB1: dimer dissociation by disruption of Val-Leu knot.
Budiman C, Angkawidjaja C, Motoike H, Koga Y, Takano K, Kanaya S
Protein Sci 20 1755-64 (2011)
PMID: 21837652

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181140 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase Chain: A
Molecule details ›
Chain: A
Length: 88 amino acids
Theoretical weight: 9.71 KDa
Source organism: Shewanella sp. SIB1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q765B0 (Residues: 1-68; Coverage: 33%)
Gene name: fklB
Sequence domains: Domain amino terminal to FKBP-type peptidyl-prolyl isomerase

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 5 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P3221
Unit cell:
a: 39.703Å b: 39.703Å c: 101.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.234 0.232 0.276
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

A substrate preference for the rough endoplasmic reticulum resident protein FKBP22 during collagen biosynthesis.
Ishikawa et al. (2014)
7 more

1 mention without citation

Crystal structure of N-domain of FKBP22 from Shewanella sp. SIB1: dimer dissociation by disruption of Val-Leu knot.
Budiman et al. (2011)