6T5K

ECV-1 from Echinicola vietnamensis. Environmental metallo-beta-lactamases exhibit high enzymatic activity under zinc deprivation

Summary for 6T5K

Entry DOI	10.2210/pdb6t5k/pdb
Descriptor	Zn-dependent hydrolase, glyoxylase, 1,2-ETHANEDIOL, ZINC ION, ... (4 entities in total)
Functional Keywords	beta-lactamase, carbapenemase, environmental, antimicrobial protein
Biological source	Echinicola vietnamensis
Total number of polymer chains	1
Total formula weight	26834.67
Authors	Frohlich, C. (deposition date: 2019-10-16, release date: 2020-05-27, Last modification date: 2024-01-24)
Primary citation	Frohlich, C.,Sorum, V.,Huber, S.,Samuelsen, O.,Berglund, F.,Kristiansson, E.,Kotsakis, S.D.,Marathe, N.P.,Larsson, D.G.J.,Leiros, H.S. Structural and biochemical characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1. J.Antimicrob.Chemother., 75:2554-2563, 2020 Cited by PubMed Abstract: MBLs form a large and heterogeneous group of bacterial enzymes conferring resistance to β-lactam antibiotics, including carbapenems. A large environmental reservoir of MBLs has been identified, which can act as a source for transfer into human pathogens. Therefore, structural investigation of environmental and clinically rare MBLs can give new insights into structure-activity relationships to explore the role of catalytic and second shell residues, which are under selective pressure. PubMed: 32464640 DOI: 10.1093/jac/dkaa175 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.33 Å)

Structure validation