3hha Summary


Crystal structure of cathepsin L in complex with AZ12878478

The structure was published by Asaad, N., Bethel, P.A., Coulson, M.D., et al., Krapp, S., Simader, H., and Steinbacher, S., in 2009 in a paper entitled "Dipeptidyl nitrile inhibitors of Cathepsin L." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.27 Å and deposited in 2009.

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

This PDB entry contains multiple copies of the structure of Cathepsin L1.

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 L1 P07711 (114-333) (CATL1_HUMAN)search Homo sapienssearch 99% 220 100%
B Cathepsin L1 P07711 (114-333) (CATL1_HUMAN)search Homo sapienssearch 99% 220 100%
C Cathepsin L1 P07711 (114-333) (CATL1_HUMAN)search Homo sapienssearch 99% 220 100%
D Cathepsin L1 P07711 (114-333) (CATL1_HUMAN)search Homo sapienssearch 99% 220 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P07711 (114 - 333) Cathepsin L1 Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P07711) Cysteine proteinasessearch PF00112: Papain family cysteine proteasesearch

Chain ID Biological process (GO) Molecular function (GO)
A, B, C, D (P07711) proteolysissearch cysteine-type peptidase activitysearch

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