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PDBsum entry 3rda

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protein ligands links
Isomerase/isomerase inhibitor PDB id
3rda
Jmol
Contents
Protein chain
164 a.a.
Ligands
MIO ×7
Waters ×415
PDB id:
3rda
Name: Isomerase/isomerase inhibitor
Title: Human cyclophilin d complexed with a fragment
Structure: Peptidyl-prolyl cis-trans isomerase f, mitochondr chain: x. Fragment: unp residues 43-207. 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:
1.07Å     R-factor:   0.116     R-free:   0.138
Authors: L.Colliandre,H.Ahmed-Belkacem,Y.Bessin,J.M.Pawlotsky,J.F.Gui
Key ref: L.Colliandre et al. Rational design of small-Molecule inhibitors of human cyclophilins and hcv replication. To be published, .
Date:
01-Apr-11     Release date:   21-Mar-12    
PROCHECK
Go to PROCHECK summary
 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)
Bound ligand (Het Group name = MIO)
matches with 46.15% similarity
= 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