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PDBsum entry 3qyu

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protein links
Isomerase PDB id
3qyu
Jmol
Contents
Protein chain
164 a.a.
Waters ×120
PDB id:
3qyu
Name: Isomerase
Title: Crystal structure of human cyclophilin d at 1.54 a resolutio temperature
Structure: Peptidyl-prolyl cis-trans isomerase f. Chain: a. Fragment: catalytic domain. Synonym: ppiase f, cyclophilin f, rotamase f. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ppif, cyp3. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.54Å     R-factor:   0.150     R-free:   0.189
Authors: L.Colliandre,M.Gelin,G.Labesse,J.-F.Guichou
Key ref: A.le Maire et al. (2011). In-plate protein crystallization, in situ ligand soaking and X-ray diffraction. Acta Crystallogr D Biol Crystallogr, 67, 747-755. PubMed id: 21904027 DOI: 10.1107/S0907444911023249
Date:
04-Mar-11     Release date:   24-Aug-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P30405  (PPIF_HUMAN) -  Peptidyl-prolyl cis-trans isomerase F, mitochondrial
Seq:
Struc:
207 a.a.
164 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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!
  Biological process     protein folding   2 terms 
  Biochemical function     peptidyl-prolyl cis-trans isomerase activity     1 term  

 

 
    Added reference    
 
 
DOI no: 10.1107/S0907444911023249 Acta Crystallogr D Biol Crystallogr 67:747-755 (2011)
PubMed id: 21904027  
 
 
In-plate protein crystallization, in situ ligand soaking and X-ray diffraction.
A.le Maire, M.Gelin, S.Pochet, F.Hoh, M.Pirocchi, J.F.Guichou, J.L.Ferrer, G.Labesse.
 
  ABSTRACT  
 
No abstract given.