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PDBsum entry 2oju

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protein Protein-protein interface(s) links
Isomerase/immunosuppressant PDB id
2oju
Jmol
Contents
Protein chains
163 a.a. *
11 a.a. *
Waters ×32
* Residue conservation analysis
PDB id:
2oju
Name: Isomerase/immunosuppressant
Title: X-ray structure of complex of human cyclophilin j with cyclo
Structure: Peptidyl-prolyl cis-trans isomerase-like 3. Chain: a, b. Synonym: ppiase, rotamase, cyclophilin-like protein ppil3, cyclophilin j, cypj. Engineered: yes. Cyclosporin a. Chain: c, d. Synonym: ciclosporin, ciclosporine. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: fetal brain. Gene: ppil3b. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Tolypocladium inflatum.
Resolution:
2.40Å     R-factor:   0.193     R-free:   0.237
Authors: Z.Xia,L.Huang
Key ref: J.Chen et al. Targeting cyclophilin j, A novel peptidyl-Prolyl isomerase, Can induce cellular g1/s arrest and repress the growth of hepatocellular carcinoma. To be published, .
Date:
14-Jan-07     Release date:   22-Jan-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9H2H8  (PPIL3_HUMAN) -  Peptidyl-prolyl cis-trans isomerase-like 3
Seq:
Struc:
161 a.a.
163 a.a.
Protein chains
No UniProt id for this chain
Struc: 11 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: Chains A, B: 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     catalytic step 2 spliceosome   2 terms 
  Biological process     protein folding   5 terms 
  Biochemical function     protein binding     3 terms