7KB1
Complex of O-acety-L-homoserine aminocarboxypropyltransferase (MetY) from Thermotoga maritima and a key reaction intermediate
Summary for 7KB1
Entry DOI | 10.2210/pdb7kb1/pdb |
Related | 7KB0 |
Descriptor | O-acetyl-L-homoserine sulfhydrylase, (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid, SODIUM ION, ... (7 entities in total) |
Functional Keywords | thermotoga maritima, methionine biosynthesis, enzyme kinetics, o-acety-l-homoserine aminocarboxypropyltransferase, mety, active site, transferase |
Biological source | Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) |
Total number of polymer chains | 4 |
Total formula weight | 189780.36 |
Authors | Brewster, J.L.,Pachl, P.,Squire, C.,Selmer, M.,Patrick, W.M. (deposition date: 2020-10-01, release date: 2021-06-23, Last modification date: 2024-04-03) |
Primary citation | Brewster, J.L.,Pachl, P.,McKellar, J.L.O.,Selmer, M.,Squire, C.J.,Patrick, W.M. Structures and kinetics of Thermotoga maritima MetY reveal new insights into the predominant sulfurylation enzyme of bacterial methionine biosynthesis. J.Biol.Chem., 296:100797-100797, 2021 Cited by PubMed: 34019879DOI: 10.1016/j.jbc.2021.100797 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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