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Ligands
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2Q6 Methyl [(2s)-2-[4-({5-[4-({(2s)-2-[(3s)-3-amino-2-oxopiperidin-1-yl]-2-cyclohexylacetyl}amino)phenyl]pentyl}oxy)phenyl]-3-(quinolin-3-yl)propyl]carbamate
ZN Zinc ion
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Code : 4PF9   PDBj   RCSB PDB   PDBe
Header : Hydrolase/Hydrolase Inhibitor
Title : Crystal structure of insulin degrading enzyme complexed with inhibitor
Release Data : 2015-06-17
Compound :
mol_id molecule chains synonym
1 Insulin-degrading enzyme A,B Abeta-degrading protease,Insulin protease,Insulinase,Insulysin
ec: 3.4.24.56
fragment: UNP residues 42-1019
mutation: C110L, E111Q, C171S, C178A, C257V, C414L, C573N, C590S, C789S, C812A, C819A, C904S, C966N, C974A
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: IDE
Authors : Wang, Y., Guo, S.
Keywords : HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.50 Å )
Citation :

Dual Exosite-binding Inhibitors of Insulin-degrading Enzyme Challenge Its Role as the Primary Mediator of Insulin Clearance in Vivo.

Durham, T.B.,Toth, J.L.,Klimkowski, V.J.  et al.
(2015)  J.Biol.Chem.  290 : 20044 - 20059

PubMed: 26085101
DOI: 10.1074/jbc.M115.638205

Chain : A, B
UniProt : P14735 (IDE_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Degradation of insulin, glucagon and other polypeptides. No action on proteins. 3.4.24.56 PubMed:10684867, PubMed:17051221, PubMed:17613531, PubMed:18986166, PubMed:19321446, PubMed:21098034, PubMed:2293021, PubMed:23922390, PubMed:24847884, PubMed:26394692, PubMed:29596046
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