7MGN
Crystal structure of F501H/H506E variant of 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) from Xanthobacter autotrophicus
Summary for 7MGN
Entry DOI | 10.2210/pdb7mgn/pdb |
Descriptor | 2-oxopropyl-CoM reductase, carboxylating, 1-THIOETHANESULFONIC ACID, DIHYDROFLAVINE-ADENINE DINUCLEOTIDE, ... (5 entities in total) |
Functional Keywords | carboxylation, oxidation-reduction, carbon dioxide fixation, carbon-carbon bond, anion-binding, kinetics, oxidoreductase |
Biological source | Xanthobacter autotrophicus PY2 |
Total number of polymer chains | 2 |
Total formula weight | 116700.71 |
Authors | Zadvornyy, O.A.,Prussia, G.,Peters, J.W. (deposition date: 2021-04-12, release date: 2021-07-21, Last modification date: 2023-10-18) |
Primary citation | Prussia, G.A.,Shisler, K.A.,Zadvornyy, O.A.,Streit, B.R.,DuBois, J.L.,Peters, J.W. The unique Phe-His dyad of 2-ketopropyl coenzyme M oxidoreductase/carboxylase selectively promotes carboxylation and S-C bond cleavage. J.Biol.Chem., 297:100961-100961, 2021 Cited by PubMed: 34265301DOI: 10.1016/j.jbc.2021.100961 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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