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PDBsum entry 4qib

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protein ligands links
Isomerase PDB id
4qib

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
145 a.a.
Ligands
PE4
SO4 ×4
Waters ×202
PDB id:
4qib
Name: Isomerase
Title: Oxidation-mediated inhibition of the peptidyl-prolyl isomerase pin1
Structure: Peptidyl-prolyl cis-trans isomerase nima-interacting 1. Chain: a. Synonym: peptidyl-prolyl cis-trans isomerase pin1, ppiase pin1, rotamase pin1. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pin1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.87Å     R-factor:   0.156     R-free:   0.185
Authors: B.T.Innes,M.A.Sowole,L.Konermann,D.W.Litchfield,C.J.Brandl, B.H.Shilton
Key ref: B.T.Innes et al. (2015). Peroxide-mediated oxidation and inhibition of the peptidyl-prolyl isomerase Pin1. Biochim Biophys Acta, 1852, 905-912. PubMed id: 25595659 DOI: 10.1016/j.bbadis.2014.12.025
Date:
30-May-14     Release date:   04-Feb-15    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q13526  (PIN1_HUMAN) -  Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 from Homo sapiens
Seq:
Struc:
163 a.a.
145 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: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Peptidylproline (omega=180)
= peptidylproline (omega=0)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1016/j.bbadis.2014.12.025 Biochim Biophys Acta 1852:905-912 (2015)
PubMed id: 25595659  
 
 
Peroxide-mediated oxidation and inhibition of the peptidyl-prolyl isomerase Pin1.
B.T.Innes, M.A.Sowole, L.Gyenis, M.Dubinsky, L.Konermann, D.W.Litchfield, C.J.Brandl, B.H.Shilton.
 
  ABSTRACT  
 
No abstract given.

 

 

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