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PDBsum entry 1fkg

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protein ligands links
Cis-trans isomerase PDB id
1fkg
Jmol
Contents
Protein chain
107 a.a. *
Ligands
SB3
Waters ×261
* Residue conservation analysis
PDB id:
1fkg
Name: Cis-trans isomerase
Title: Design, synthesis, and kinetic evaluation of high-affinity fkbp ligands, and the x-ray crystal structures of their complexes with fkbp12
Structure: Fk506 binding protein. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
Resolution:
2.00Å     R-factor:   0.184    
Authors: D.A.Holt,J.I.Luengo,D.S.Yamashita,H.-J.Oh,A.L.Konialian,H.- K.Yen,L.W.Rozamus,M.Brandt,M.J.Bossard,M.A.Levy, D.S.Eggleston,T.J.Stout,J.Liang,L.W.Schultz,J.Clardy
Key ref: D.A.Holt et al. (1993). Design, Synthesis, And kinetic evaluation of high-Affinity fkbp ligands and the X-Ray crystal-Structures of their complexes with fkbp12.. J.Am.Chem.Soc., 115, 9925-9938.
Date:
05-Aug-93     Release date:   31-Jan-94    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P62942  (FKB1A_HUMAN) -  Peptidyl-prolyl cis-trans isomerase FKBP1A
Seq:
Struc:
108 a.a.
107 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     membrane   7 terms 
  Biological process     regulation of immune response   24 terms 
  Biochemical function     ion channel binding     14 terms