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PDBsum entry 1zkf

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protein ligands Protein-protein interface(s) links
Isomerase/isomerase substrate PDB id
1zkf
Jmol PyMol
Contents
Protein chains
165 a.a. *
Ligands
SIN-ALA-GLY-PRO-
PHE-NIT
×2
Waters ×90
* Residue conservation analysis
PDB id:
1zkf
Name: Isomerase/isomerase substrate
Title: Cyrstal structure of human cyclophilin-a in complex with suc
Structure: Peptidyl-prolyl cis-trans isomerase a. Chain: a, b. Synonym: ppiase, rotamase, cyclophilin a, cyclosporin a-bin protein. Engineered: yes. Suc-ala-gly-pro-phe-pna. Chain: c, d. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ppia, cypa. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: the peptide substrate was purchased from bac of prussia, pa).
Biol. unit: Tetramer (from PQS)
Resolution:
2.55Å     R-factor:   0.168     R-free:   0.210
Authors: E.Z.Eisenmesser,V.Thai,E.Pozharski,D.Kern
Key ref: E.Z.Eisenmesser et al. Mechanistic insights of cyclophilin-A from X-Ray cyrstallographic and nuclear magnet resonance investigations. To be published, .
Date:
02-May-05     Release date:   11-Apr-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P62937  (PPIA_HUMAN) -  Peptidyl-prolyl cis-trans isomerase A
Seq:
Struc:
165 a.a.
165 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     extracellular region   10 terms 
  Biological process     viral reproduction   17 terms 
  Biochemical function     protein binding     6 terms  

 

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