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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
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
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 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   8 terms 
  Biological process     viral reproduction   18 terms 
  Biochemical function     protein binding     7 terms