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PDBsum entry 3k2c
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protein ligands Protein-protein interface(s) links
Isomerase PDB id
3k2c

 

 

 

 

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Contents
Protein chains
174 a.a. *
Ligands
PG5 ×2
EDO ×2
SO4 ×2
Waters ×438
* Residue conservation analysis
PDB id:
3k2c
Name: Isomerase
Title: Crystal structure of peptidyl-prolyl cis-trans isomerase from encephalitozoon cuniculi at 1.9 a resolution
Structure: Peptidyl-prolyl cis-trans isomerase. Chain: a, b, c, d. Synonym: ppiase, rotamase, cyclophilin, cph. Engineered: yes
Source: Encephalitozoon cuniculi. Microsporidian parasite. Organism_taxid: 6035. Gene: cpr1, ecu08_0470. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.95Å     R-factor:   0.166     R-free:   0.216
Authors: Ssgcid,Seattle Structural Genomics Center For Infectious Disease (Ssgcid)
Key ref: Ssgcid et al. Crystal structure of peptidyl-Prolyl cis-Trans isomerase from encephalitozoon cuniculi at 1.9 a resolution. To be published, .
Date:
29-Sep-09     Release date:   13-Oct-09    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8SRE1  (CYPH_ENCCU) -  Peptidyl-prolyl cis-trans isomerase from Encephalitozoon cuniculi (strain GB-M1)
Seq:
Struc: 		172 a.a.
174 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.5.2.1.8  - peptidylprolyl isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Peptidylproline (omega=180)
 = peptidylproline (omega=0)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

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