1m6d Summary


Crystal structure of human cathepsin F

The structure was published by Somoza, J.R., Palmer, J.T., and Ho, J.D., in 2002 in a paper entitled "The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2002.

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

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

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 F Q9UBX1 (271-484) (CATF_HUMAN)search Homo sapienssearch < 90% 214 100%
B Cathepsin F Q9UBX1 (271-484) (CATF_HUMAN)search Homo sapienssearch < 90% 214 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9UBX1 (271 - 484) Cathepsin F Homo sapiens

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

Chain ID Molecular function (GO) Biological process (GO)
A, B (Q9UBX1) cysteine-type peptidase activitysearch proteolysissearch

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