› 3ich

X-ray diffraction
1.2Å resolution

Crystal structure of cyclophilin B at 1.2 A resolution

Released:
DOI: 10.2210/pdb3ich/pdb
PDB entry 3ich coloured by chain, front view.
PDB entry 3ich coloured by chain, side view.
PDB entry 3ich coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain.
Kozlov G, Bastos-Aristizabal S, Määttänen P, Rosenauer A, Zheng F, Killikelly A, Trempe JF, Thomas DY, Gehring K
J Biol Chem 285 35551-7 (2010)
PMID: 20801878

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149921 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase B Chain: A
Molecule details ›
Chain: A
Length: 188 amino acids
Theoretical weight: 20.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P23284 (Residues: 34-216; Coverage: 100%)
Gene names: CYPB, PPIB
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: P32
Unit cell:
a: 64.665Å b: 64.665Å c: 39.463Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.144 0.143 0.162
Expression system: Escherichia coli BL21

Quick links

Citations

19 review citations

Protein folding in the endoplasmic reticulum.
Braakman et al. (2013)
18 more

8 mentions without citation

Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain.
Kozlov et al. (2010)
7 more