8PCH

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

Summary for 8PCH

Entry DOI	10.2210/pdb8pch/pdb
Descriptor	CATHEPSIN H, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywords	hydrolase, protease, cysteine proteinase, aminopeptidase
Biological source	Sus scrofa (pig) More
Total number of polymer chains	2
Total formula weight	25763.94
Authors	Guncar, G.,Podobnik, M.,Pungercar, J.,Strukelj, B.,Turk, V.,Turk, D. (deposition date: 1997-11-07, release date: 1998-12-09, Last modification date: 2023-08-09)
Primary citation	Guncar, G.,Podobnik, M.,Pungercar, J.,Strukelj, B.,Turk, V.,Turk, D. 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. Structure, 6:51-61, 1998 Cited by PubMed Abstract: Cathepsin H is a lysosomal cysteine protease, involved in intracellular protein degradation. It is the only known mono-aminopeptidase in the papain-like family and is reported to be involved in tumor metastasis. The cathepsin H structure was determined in order to investigate the structural basis for its aminopeptidase activity and thus to provide the basis for structure-based design of synthetic inhibitors. PubMed: 9493267 DOI: 10.1016/S0969-2126(98)00007-0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation