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6MFI

MIM-2 Metallo-Beta-Lactamase

Summary for 6MFI
Entry DOI10.2210/pdb6mfi/pdb
DescriptorMetallo-beta-lactamase, ZINC ION (3 entities in total)
Functional Keywordsmetallohydrolase, hydrolase, b3
Biological sourceSimiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1)
Total number of polymer chains1
Total formula weight31488.18
Authors
Selleck, C.,Guddat, L.,Schenk, G.,Monteiro Pedroso, M. (deposition date: 2018-09-11, release date: 2019-11-13, Last modification date: 2024-11-20)
Primary citationSelleck, C.,Clayton, D.,Gahan, L.R.,Mitic, N.,McGeary, R.P.,Pedroso, M.M.,Guddat, L.W.,Schenk, G.,Monteiro Pedroso, M.
characterization of the B3 MBLs MIM-1 and MIM-2 from environmental microorganisms.
Chemistry, 23:4778-4781, 2017
Cited by
PubMed Abstract: Metallohydrolases are a vast family of enzymes that play crucial roles in numerous metabolic pathways. Several members have emerged as targets for chemotherapeutics. Knowledge about their reaction mechanisms and associated transition states greatly aids the design of potent and highly specific drug leads. By using a high-resolution crystal structure, we have probed the trajectory of the reaction catalyzed by purple acid phosphatase, an enzyme essential for the integrity of bone structure. In particular, the transition state is visualized, thus providing detailed structural information that may be exploited in the design of specific inhibitors for the development of new anti-osteoporotic chemotherapeutics.
PubMed: 28261912
DOI: 10.1002/chem.201700866
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.839 Å)
Structure validation

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