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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>

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( jV3 / Jmol ) *1
PDB ID2djg  sequence information (FASTA format)   
RELATED PDB ID1k3b, 1jqp, 2djf
DescriptorDipeptidyl-peptidase 1 (E.C.3.4.14.1)
TitleRe-determination of the native structure of human dipeptidyl peptidase I (cathepsin C)
Functional Keywordsre-refinement, cysteine protease, cathepsin C, dipeptidyl peptidase I, Hydrolase
Biological sourceHomo sapiens (human)
Cellular location [UNP - P53634] Lysosome
Organ source [UNP - P53634] Ileum
[UNP - P53634] Blood
[UNP - P53634] Rheumatoid arthritic synovial fluid
[UNP - P53634] Thyroid
[UNP - P53634] Spleen
Total number of polymer chains4
Total molecular weight41156.7 (the details in Structural Details Page)
AuthorsMolgaard, A. , Arnau, J. , Lauritzen, C. , Larsen, S. , Petersen, G. , Pedersen, J. (deposition date : 2006-04-02, release date : 2006-11-14)
Primary citationMolgaard, A. , Arnau, J. , Lauritzen, C. , Larsen, S. , Petersen, G. , Pedersen, J.
The crystal structure of human dipeptidyl peptidase I (cathepsin C) in complex with the inhibitor Gly-Phe-CHN2
Biochem.J., 401:645 - 650, 2007.(PubMed : 17020538)  (DOI: 10.1042/BJ20061389)
Experimental methodX-RAY DIFFRACTION ( 2.05[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P53634 ) , eF-site , KEGG ( EC 3.4.14.1 ) , PISA