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PDBsum entry 2alf

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protein metals links
Isomerase PDB id
2alf
Jmol
Contents
Protein chain
164 a.a. *
Metals
_MG
Waters ×245
* Residue conservation analysis
PDB id:
2alf
Name: Isomerase
Title: Crystal structure of human cypa mutant k131a
Structure: Peptidyl-prolyl cis-trans isomerase a. Chain: a. Synonym: ppiase, rotamase, cyclophilin a, cyclosporin a- binding protein. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: cypa. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
1.90Å     R-factor:   0.193     R-free:   0.226
Authors: H.Hu,C.-Q.Huang,H.-L.Liu,Y.Han,M.-E.Chen,L.Yu,R.-C.Bi
Key ref: H.Hu et al. Nuclease activity of cyclophilin a and its structural basis. To be published, .
Date:
05-Aug-05     Release date:   23-Aug-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P62937  (PPIA_HUMAN) -  Peptidyl-prolyl cis-trans isomerase A
Seq:
Struc:
165 a.a.
164 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 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