2xu3 Summary



The structure was published by Hardegger, L.A., Kuhn, B., Spinnler, B., et al., Banner, D.W., Haap, W., and Diederich, F., in 2011 in a paper entitled "Systematic Investigation of Halogen Bonding in Protein-Ligand Interactions." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 0.9 Å and deposited in 2010.

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

The PDB entry contains the structure of CATHEPSIN L1. This molecule has the UniProt identifier P07711 (CATL1_HUMAN)search. The sample contained 220 residues which is < 90% of the natural sequence. Out of 220 residues 220 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 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 (P07711) Cysteine proteinasessearch PF00112: Papain family cysteine proteasesearch

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

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