1qdq Summary

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X-RAY CRYSTAL STRUCTURE OF BOVINE CATHEPSIN B-CA074 COMPLEX

The structure was published by Yamamoto, A., Tomoo, K., Hara, T., Murata, M., Kitamura, K., and Ishida, T., in 2000 in a paper entitled "Substrate specificity of bovine cathepsin B and its inhibition by CA074, based on crystal structure refinement of the complex." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.18 Å and deposited in 1999.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of CATHEPSIN B. This molecule has the UniProt identifier P07688 (CATB_BOVIN)search. The sample contained 253 residues which is < 90% of the natural sequence. Out of 253 residues 251 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 is most likely monomeric.

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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A CATHEPSIN B P07688 (80-332) (CATB_BOVIN)search Bos taurussearch < 90% 253 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P07688 (80 - 332) CATHEPSIN B Bos taurus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Papain-likesearch Cysteine proteinasessearch Papain family cysteine proteasesearch

Chain ID Biological process (GO) Molecular function (GO)
A (P07688) proteolysissearch cysteine-type peptidase activitysearch

Chain InterPro annotation
A Cysteine peptidase, cysteine active sitesearch Peptidase C1A, papain C-terminalsearch Peptidase C1Asearch Peptidase C1A, cathepsin Bsearch Cysteine peptidase, histidine active sitesearch Cysteine peptidase, asparagine active sitesearch