2CB5

HUMAN BLEOMYCIN HYDROLASE, C73S/DELE455 MUTANT

Summary for 2CB5

• Entry DOI: 10.2210/pdb2cb5/pdb
• Related: 1CB5
• Descriptor: PROTEIN (BLEOMYCIN HYDROLASE) (2 entities in total)
• Functional Keywords: hydrolase, aminopeptidase, cysteine protease, self-compartmentalizing, bleomycin, cylinase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q13867
• Total number of polymer chains: 2
• Total formula weight: 104655.34

Authors

O'Farrell, P.A.,Gonzalez, F.,Zheng, W.,Johnston, S.A.,Joshua-Tor, L. (deposition date: 1999-03-02, release date: 2000-03-06, Last modification date: 2023-08-23)

Primary citation

O'Farrell, P.A.,Gonzalez, F.,Zheng, W.,Johnston, S.A.,Joshua-Tor, L.
Crystal structure of human bleomycin hydrolase, a self-compartmentalizing cysteine protease.
Structure Fold.Des., 7:619-627, 1999

PubMed Abstract: Bleomycin hydrolase (BH) is a cysteine protease that is found in all tissues in mammals as well as in many other eukaryotes and prokaryotes. Although its conserved cellular function is as yet unknown, human bleomycin hydrolase (hBH) has clinical significance in that it is thought to be the major cause of tumor cell resistance to bleomycin chemotherapy. In addition, it has been reported that an allelic variant of hBH is genetically linked to Alzheimer's disease.

PubMed: 10404591
DOI: 10.1016/S0969-2126(99)80083-5

Experimental method

X-RAY DIFFRACTION (1.85 Å)