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Ligands
Code Name Style Show Link
C8S (2s)-2-amino-1-[(1s,3s,5s)-3-(aminomethyl)-2-azabicyclo[3.1.0]hexan-2-yl]-2-[(1r,3r,5s,7s)-3,5-dihydroxytricyclo[3.3.1.1~3,7~]decan-1-yl]ethan-1-one
Non-standard Residues
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Glycosylation
Code Name Emphasize
NAG 2-acetamido-2-deoxy-beta-D-glucopyranose
Modification
Code Name Show
Code : 6B1O   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE Inhibitor
Title : The structure of DPP4 in complex with Vildagliptin Analog
Release Data : 2017-09-27
Compound :
mol_id molecule chains synonym
1 Dipeptidyl peptidase 4 A,B ADABP,Adenosine deaminase complexing protein 2,ADCP-2,Dipeptidyl peptidase IV,DPP IV,T-cell activation antigen CD26,TP103
ec: 3.4.14.5
mutation: S39T
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Spodoptera frugiperda  (taxid:7108)
gene: DPP4, ADCP2, CD26
Authors : Scapin, G.
Keywords : Diabetes, DPP4 inhibitors, covalent inhibitors, HYDROLASE, HYDROLASE-HYDROLASE Inhibitor complex
Exp. method : X-RAY DIFFRACTION ( 1.9100 Å )
Citation :

A comparative study of the binding properties, dipeptidyl peptidase-4 (DPP-4) inhibitory activity and glucose-lowering efficacy of the DPP-4 inhibitors alogliptin, linagliptin, saxagliptin, sitagliptin and vildagliptin in mice.

Berger, J.P.,SinhaRoy, R.,Pocai, A.  et al.
(2018)  Endocrinol Diabetes Metab  1 : e00002 - e00002

PubMed: 30815539
DOI: 10.1002/edm2.2

Chain : A, B
UniProt : P27487 (DPP4_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. 3.4.14.5 PROSITE- ProRule:PRU10084, PubMed:10593948
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