The structure of DPP4 in complex with Vildagliptin Analog

Summary for 6B1O

DescriptorDipeptidyl peptidase 4, N-ACETYL-D-GLUCOSAMINE, (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[,7~]decan-1-yl]ethan-1-one, ... (4 entities in total)
Functional Keywordsdiabetes, dpp4 inhibitors, covalent inhibitors, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total molecular weight174269.55
Scapin, G. (deposition date: 2017-09-18, release date: 2017-09-27, Last modification date: 2019-03-13)
Primary citation
Berger, J.P.,SinhaRoy, R.,Pocai, A.,Kelly, T.M.,Scapin, G.,Gao, Y.D.,Pryor, K.A.D.,Wu, J.K.,Eiermann, G.J.,Xu, S.S.,Zhang, X.,Tatosian, D.A.,Weber, A.E.,Thornberry, N.A.,Carr, R.D.
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.
Endocrinol Diabetes Metab, 1:e00002-e00002, 2018
PubMed: 30815539 (PDB entries with the same primary citation)
DOI: 10.1002/edm2.2
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.20520 2.1% 3.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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