1K3B

Crystal Structure of Human Dipeptidyl Peptidase I (Cathepsin C): Exclusion Domain Added to an Endopeptidase Framework Creates the Machine for Activation of Granular Serine Proteases

Summary for 1K3B

Descriptordipeptydil-peptidase I exclusion domain, dipeptydil-peptidase I light chain, dipeptydil-peptidase I heavy chain, ... (7 entities in total)
Functional Keywordshydrolase
Biological sourceHomo sapiens (human)
Cellular locationLysosome P53634 P53634 P53634
Total number of polymer chains3
Total molecular weight40120.33
Authors
Turk, D.,Janjic, V.,Stern, I.,Podobnik, M.,Lamba, D.,Dahl, S.W.,Lauritzen, C.,Pedersen, J.,Turk, V.,Turk, B. (deposition date: 2001-10-02, release date: 2002-04-02, Last modification date: 2011-07-13)
Primary citation
Turk, D.,Janjic, V.,Stern, I.,Podobnik, M.,Lamba, D.,Dahl, S.W.,Lauritzen, C.,Pedersen, J.,Turk, V.,Turk, B.
Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases.
EMBO J., 20:6570-6582, 2001
PubMed: 11726493 (PDB entries with the same primary citation)
DOI: 10.1093/emboj/20.23.6570
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.15 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers122.3%7.1%6.5%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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