3mpf Summary

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Crystal structure of human Cathepsin-S C25S mutant with bound drug

The structure was published by Ameriks, M.K., Bembenek, S.D., Burdett, M.T., et al., Sun, S., Thurmond, R.L., and Zhu, J., in 2010 in a paper entitled "Diazinones as P2 replacements for pyrazole-based cathepsin S inhibitors" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2010.

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

This PDB entry contains multiple copies of the structure of Cathepsin S.

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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Cathepsin S P25774 (115-331) (CATS_HUMAN)search Homo sapienssearch 100% 219 100%
B Cathepsin S P25774 (115-331) (CATS_HUMAN)search Homo sapienssearch 100% 219 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P25774 (115 - 331) Cathepsin S Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A, B (P25774) Cysteine proteinasessearch PF00112: Papain family cysteine proteasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P25774) cysteine-type peptidase activitysearch proteolysissearch

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