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PDBsum entry 4pf7

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protein ligands metals Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
4pf7

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
955 a.a.
Ligands
2QW ×2
Metals
_ZN ×2
Waters ×578
PDB id:
4pf7
Name: Hydrolase/hydrolase inhibitor
Title: Crystal structure of insulin degrading enzyme complexed with inhibitor
Structure: Insulin-degrading enzyme. Chain: a, b. Fragment: unp residues 42-1019. Synonym: abeta-degrading protease,insulin protease,insulinase, insulysin. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ide. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.33Å     R-factor:   0.199     R-free:   0.236
Authors: Y.Wang,S.Guo
Key ref: T.B.Durham et al. (2015). Dual Exosite-binding Inhibitors of Insulin-degrading Enzyme Challenge Its Role as the Primary Mediator of Insulin Clearance in Vivo. J Biol Chem, 290, 20044-20059. PubMed id: 26085101 DOI: 10.1074/jbc.M115.638205
Date:
28-Apr-14     Release date:   17-Jun-15    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P14735  (IDE_HUMAN) -  Insulin-degrading enzyme from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
1019 a.a.
955 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 12 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.4.24.56  - insulysin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Degradation of insulin, glucagon and other polypeptides. No action on proteins.
      Cofactor: Zn(2+)

 

 
DOI no: 10.1074/jbc.M115.638205 J Biol Chem 290:20044-20059 (2015)
PubMed id: 26085101  
 
 
Dual Exosite-binding Inhibitors of Insulin-degrading Enzyme Challenge Its Role as the Primary Mediator of Insulin Clearance in Vivo.
T.B.Durham, J.L.Toth, V.J.Klimkowski, J.X.Cao, A.M.Siesky, J.Alexander-Chacko, G.Y.Wu, J.T.Dixon, J.E.McGee, Y.Wang, S.Y.Guo, R.N.Cavitt, J.Schindler, S.J.Thibodeaux, N.A.Calvert, M.J.Coghlan, D.K.Sindelar, M.Christe, V.V.Kiselyov, M.D.Michael, K.W.Sloop.
 
  ABSTRACT  
 
No abstract given.

 

 

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