7V5S
Crystal structure of human bleomycin hydrolase C73A mutant
Summary for 7V5S
| Entry DOI | 10.2210/pdb7v5s/pdb |
| Descriptor | Bleomycin hydrolase, TETRAETHYLENE GLYCOL, TRIETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | cysteine protease, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 55111.79 |
| Authors | Chang, C.Y.,Zheng, Y.Z.,Huang, S.J.,Wang, Y.L.,Toh, S.I.,Lin, E.C. (deposition date: 2021-08-18, release date: 2022-06-29, Last modification date: 2023-11-29) |
| Primary citation | Zheng, Y.Z.,Cui, J.,Wang, Y.L.,Huang, S.J.,Lin, E.C.,Huang, S.C.,Rudolf, J.D.,Yan, X.,Chang, C.Y. The Structure-Function Relationship of Human Bleomycin Hydrolase: Mutation of a Cysteine Protease into a Serine Protease. Chembiochem, 23:e202200186-e202200186, 2022 Cited by PubMed Abstract: Human bleomycin hydrolase (hBH) catalyzes deamidation of the anticancer drug bleomycins (BLM). This enzyme is involved in BLM detoxification and drug resistance. Herein, we report the putative BLM-binding site and catalytic mechanism of hBH. The crystal structures and biochemical studies suggest that hBH cleaves its C-terminal residue without significant preference for the type of amino acid, and therefore can accordingly accommodate the β-aminoalanine amide moiety of BLM for deamidation. Interestingly, hBH is capable of switching from a cysteine protease to a serine protease that is unable to cleave the secondary amide of hBH C-terminus but reacts with the primary amide of BLMs. PubMed: 35467071DOI: 10.1002/cbic.202200186 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.02 Å) |
Structure validation
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