Crystal Structure of Dipeptidyl Aminopeptidase IV from Stenotrophomonas maltophilia

Summary for 2ECF

DescriptorDipeptidyl peptidase IV (2 entities in total)
Functional Keywordsprolyl oligopeptidase family, peptidase family s9, dipeptidyl peptidase iv, hydrolase
Biological sourceStenotrophomonas maltophilia
Total number of polymer chains1
Total molecular weight82180.33
Nakajima, Y.,Ito, K.,Yoshimoto, T. (deposition date: 2007-02-13, release date: 2008-02-26, Last modification date: 2011-07-13)
Primary citation
Nakajima, Y.,Ito, K.,Toshima, T.,Egawa, T.,Zheng, H.,Oyama, H.,Wu, Y.-F.,Takahashi, E.,Kyono, K.,Yoshimoto, T.
Dipeptidyl aminopeptidase IV from Stenotrophomonas maltophilia exhibits activity against a substrate containing a 4-hydroxyproline residue
J.Bacteriol., 190:7819-7829, 2008
PubMed: 18820015 (PDB entries with the same primary citation)
DOI: 10.1128/JB.02010-07
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.238120.7%3.6%0.4%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution