1cte Summary

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CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX: IMPLICATIONS FOR STRUCTURE-BASED INHIBITOR DESIGN

The structure was published by Jia, Z., Hasnain, S., Hirama, T., et al., Mort, J.S., To, R., and Huber, C.P., in 1995 in a paper entitled "Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1995.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of CATHEPSIN B.

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 most likely forms homodimers.

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 P00787 (80-333) (CATB_RAT)search Rattus norvegicussearch 100% 254 99%
B CATHEPSIN B P00787 (80-333) (CATB_RAT)search Rattus norvegicussearch 100% 254 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00787 (80 - 333) CATHEPSIN B Rattus norvegicus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P00787) Papain-likesearch Cysteine proteinasessearch PF00112: Papain family cysteine proteasesearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (P00787) proteolysissearch cysteine-type peptidase activitysearch

Chain InterPro annotation
A, B 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