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PDBsum entry 3ici

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protein ligands metals Protein-protein interface(s) links
Isomerase PDB id
3ici
Jmol
Contents
Protein chains
187 a.a. *
Ligands
ASP-TRP-ASN-GLU-
ASP-MET-ASP-GLY-
GLU
MES
Metals
_ZN ×2
Waters ×504
* Residue conservation analysis
PDB id:
3ici
Name: Isomerase
Title: Crystal structure of cyclophilin b in complex with calmegin
Structure: Peptidyl-prolyl cis-trans isomerase b. Chain: a, b. Fragment: unp residues 34-216. Synonym: ppiase, rotamase, cyclophilin b, s-cyclophilin, sc s1. Engineered: yes. Calnexin. Chain: c. Fragment: p-domain fragment: residues 317-350.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ppib, cypb. Expressed in: escherichia coli. Expression_system_taxid: 511693. Canis lupus familiaris. Dog. Organism_taxid: 9615.
Resolution:
1.70Å     R-factor:   0.190     R-free:   0.239
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
Date:
17-Jul-09     Release date:   21-Jul-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P23284  (PPIB_HUMAN) -  Peptidyl-prolyl cis-trans isomerase B
Seq:
Struc:
216 a.a.
187 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.5.2.1.8  - 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   7 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.
 
  ABSTRACT  
 
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.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.