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PDBsum entry 3uch

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protein links
Isomerase PDB id
3uch
Jmol PyMol
Contents
Protein chain
173 a.a.
Waters ×49
PDB id:
3uch
Name: Isomerase
Title: Crystal structure of a peptidyl-prolyl cis-trans isomerase e from homo sapiens at 2.50 a resolution
Structure: Peptidyl-prolyl cis-trans isomerase e. Chain: a. Fragment: residues 129-301. Synonym: ppiase e, cyclophilin e, cyclophilin-33, rotamase engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: bc008451, cyp33, ppie. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.191     R-free:   0.214
Authors: Joint Center For Structural Genomics (Jcsg),Partnership For Biology (Tcell)
Key ref: Joint center for structural genomics (jcsg) and partnership for t-cell biology Crystal structure of a hypotherical peptidyl-Prolyl cis-Trans isomerase e (ppie) from homo sapiens at 2.5 resolution. To be published, .
Date:
26-Oct-11     Release date:   16-Nov-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9UNP9  (PPIE_HUMAN) -  Peptidyl-prolyl cis-trans isomerase E
Seq:
Struc:
301 a.a.
173 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     peptidyl-prolyl cis-trans isomerase activity     1 term  

 

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