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PDBsum entry 1vdn

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protein ligands links
Isomerase/isomerase inhibitor PDB id
1vdn
Jmol
Contents
Protein chain
161 a.a. *
Ligands
ACE-ALA-ALA-PRO-
ALA-MCM
Waters ×188
* Residue conservation analysis
PDB id:
1vdn
Name: Isomerase/isomerase inhibitor
Title: Crystal structure of yeast cyclophilin a complexed with ace- pro-ala-7-amino-4-methylcoumarin
Structure: Cyclophilin a. Chain: a. Synonym: peptidyl-prolyl cis-trans isomerase. Engineered: yes. (Ace)aapa(mcm). Chain: b. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: chemically synthesized
Biol. unit: Dimer (from PQS)
Resolution:
1.60Å     R-factor:   0.199     R-free:   0.237
Authors: M.Konno,T.Shibano,K.Okudaira,N.Takahashi
Key ref: M.Konno et al. Crystal structure of yeast cyclophilin a complexed with ace-Ala-Ala-Pro-Ala-7-Amino-4-Methylcoumarin. To be published, .
Date:
24-Mar-04     Release date:   28-Jun-05    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P14832  (CYPH_YEAST) -  Peptidyl-prolyl cis-trans isomerase
Seq:
Struc:
162 a.a.
161 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!
  Cellular component     cytoplasm   6 terms 
  Biological process     transport   8 terms 
  Biochemical function     isomerase activity     4 terms