8pch Summary

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CRYSTAL STRUCTURE OF PORCINE CATHEPSIN H DETERMINED AT 2.1 ANGSTROM RESOLUTION: LOCATION OF THE MINI-CHAIN C-TERMINAL CARBOXYL GROUP DEFINES CATHEPSIN H AMINOPEPTIDASE FUNCTION

The structure was published by Guncar, G., Podobnik, M., Pungercar, J., Strukelj, B., Turk, V., and Turk, D., in 1998 in a paper entitled "Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1997.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely CATHEPSIN H.

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 heterodimers.

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 H O46427 (116-334) (CATH_PIG)search Sus scrofasearch < 90% 220 100%
P CATHEPSIN H O46427 (98-105) (CATH_PIG)search Sus scrofasearch < 90% 8 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O46427 (116 - 334) CATHEPSIN H Sus scrofa

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

Chain ID Biological process (GO) Molecular function (GO)
A (O46427) proteolysissearch cysteine-type peptidase activitysearch

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
P