PDBsum entry 3ich

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protein links
Isomerase PDB id
Protein chain
180 a.a. *
Waters ×376
* Residue conservation analysis
PDB id:
Name: Isomerase
Title: Crystal structure of cyclophilin b at 1.2 a resolution
Structure: Peptidyl-prolyl cis-trans isomerase b. Chain: a. Fragment: unp residues 34-216. Synonym: ppiase, rotamase, cyclophilin b, s-cyclophilin, sc s1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ppib, cypb. Expressed in: escherichia coli. Expression_system_taxid: 511693.
1.20Å     R-factor:   0.144     R-free:   0.162
Authors: G.Kozlov,K.Gehring
Key ref: G.Kozlov et al. (2010). Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain. J Biol Chem, 285, 35551-35557. PubMed id: 20801878 DOI: 10.1074/jbc.M110.160101
17-Jul-09     Release date:   21-Jul-10    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P23284  (PPIB_HUMAN) -  Peptidyl-prolyl cis-trans isomerase B
216 a.a.
180 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Peptidylprolyl isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Peptidylproline (omega=180) = peptidylproline (omega=0)
Peptidylproline (omega=180)
= peptidylproline (omega=0)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     macromolecular complex   8 terms 
  Biological process     chaperone-mediated protein folding   8 terms 
  Biochemical function     protein binding     8 terms  


    Added reference    
DOI no: 10.1074/jbc.M110.160101 J Biol Chem 285:35551-35557 (2010)
PubMed id: 20801878  
Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain.
G.Kozlov, S.Bastos-Aristizabal, P.Määttänen, A.Rosenauer, F.Zheng, A.Killikelly, J.F.Trempe, D.Y.Thomas, K.Gehring.
No abstract given.


Literature references that cite this PDB file's key reference

  PubMed id Reference
21282188 S.M.Pyott, U.Schwarze, H.E.Christiansen, M.G.Pepin, D.F.Leistritz, R.Dineen, C.Harris, B.K.Burton, B.Angle, K.Kim, M.D.Sussman, M.Weis, D.R.Eyre, D.W.Russell, K.J.McCarthy, R.D.Steiner, and P.H.Byers (2011).
Mutations in PPIB (cyclophilin B) delay type I procollagen chain association and result in perinatal lethal to moderate osteogenesis imperfecta phenotypes.
  Hum Mol Genet, 20, 1595-1609.  
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