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PDBsum entry 3prb

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protein Protein-protein interface(s) links
Chaperone, isomerase PDB id
3prb
Jmol
Contents
Protein chains
223 a.a. *
Waters ×179
* Residue conservation analysis
PDB id:
3prb
Name: Chaperone, isomerase
Title: Structural analysis of protein folding by the methanococcus chaperone fkbp26
Structure: Fkbp-type peptidyl-prolyl cis-trans isomerase. Chain: a, b. Synonym: ppiase, rotamase, long-type fkbp. Engineered: yes
Source: Methanocaldococcus jannaschii. Methanococcus jannaschii. Organism_taxid: 2190. Gene: mj0825. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.20Å     R-factor:   0.229     R-free:   0.274
Authors: E.Martinez-Hackert,W.A.Hendrickson
Key ref: E.Martinez-Hackert and W.A.Hendrickson (2011). Structural analysis of protein folding by the long-chain archaeal chaperone FKBP26. J Mol Biol, 407, 450-464. PubMed id: 21262232 DOI: 10.1016/j.jmb.2011.01.027
Date:
29-Nov-10     Release date:   19-Jan-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q58235  (FKBP2_METJA) -  Putative FKBP-type peptidyl-prolyl cis-trans isomerase MJ0825
Seq:
Struc:
231 a.a.
223 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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!
  Biological process     protein folding   2 terms 
  Biochemical function     isomerase activity     2 terms  

 

 
    Added reference    
 
 
DOI no: 10.1016/j.jmb.2011.01.027 J Mol Biol 407:450-464 (2011)
PubMed id: 21262232  
 
 
Structural analysis of protein folding by the long-chain archaeal chaperone FKBP26.
E.Martinez-Hackert, W.A.Hendrickson.
 
  ABSTRACT  
 
No abstract given.