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PDBsum entry 2r99

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protein links
Isomerase PDB id
2r99
Jmol
Contents
Protein chain
164 a.a. *
Waters ×215
* Residue conservation analysis
PDB id:
2r99
Name: Isomerase
Title: Crystal structure of cyclophilin abh-like domain of human peptidylprolyl isomerase e isoform 1
Structure: Peptidyl-prolyl cis-trans isomerase e. Chain: a. Fragment: cyclophilin domain: residues 131-301. Synonym: ppiase e, rotamase e, cyclophilin e, cyclophilin 33. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ppie, cyp33. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
1.61Å     R-factor:   0.164     R-free:   0.196
Authors: J.R.Walker,T.Davis,E.M.Newman,F.Mackenzie,M.Sundstrom, C.H.Arrowsmith,A.M.Edwards,A.Bochkarev,S.Dhe-Paganon, Structural Genomics Consortium (Sgc)
Key ref: J.R.Walker et al. X-Ray crystal structure of the cyclophilin domain of human peptidylprolyl isomerase e isoform 1.. To be published, .
Date:
12-Sep-07     Release date:   25-Sep-07    
Supersedes: 1zcx
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9UNP9  (PPIE_HUMAN) -  Peptidyl-prolyl cis-trans isomerase E
Seq:
Struc:
301 a.a.
164 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!
  Biological process     protein folding   2 terms 
  Biochemical function     peptidyl-prolyl cis-trans isomerase activity     1 term