dipeptidyl peptidase I (cathepsin C), a tetrameric cysteine protease of the papain family
The structure was published by Olsen, J.G., Kadziola, A., Lauritzen, C., Pedersen, J., Larsen, S., and Dahl, S.W., in 2001 in a paper entitled "Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2001.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of dipeptidyl peptidase I. This molecule has the UniProt identifier P80067 (CATC_RAT). The sample contained 438 residues which is 100% of the natural sequence. Out of 438 residues 348 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: