2MAD
THE ACTIVE SITE STRUCTURE OF METHYLAMINE DEHYDROGENASE: HYDRAZINES IDENTIFY C6 AS THE REACTIVE SITE OF THE TRYPTOPHAN DERIVED QUINONE COFACTOR
Replaces: 1MADSummary for 2MAD
| Entry DOI | 10.2210/pdb2mad/pdb |
| Descriptor | METHYLAMINE DEHYDROGENASE (LIGHT SUBUNIT), METHYLAMINE DEHYDROGENASE (HEAVY SUBUNIT) (3 entities in total) |
| Functional Keywords | oxidoreductase(chnh2(d)-deaminating) |
| Biological source | Paracoccus versutus More |
| Cellular location | Periplasm: P22641 P23006 |
| Total number of polymer chains | 2 |
| Total formula weight | 51700.15 |
| Authors | Huizinga, E.G.,Vellieux, F.M.D.,Hol, W.G.J. (deposition date: 1992-05-20, release date: 1994-01-31, Last modification date: 2011-07-13) |
| Primary citation | Huizinga, E.G.,van Zanten, B.A.,Duine, J.A.,Jongejan, J.A.,Huitema, F.,Wilson, K.S.,Hol, W.G. Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor. Biochemistry, 31:9789-9795, 1992 Cited by PubMed: 1390754DOI: 10.1021/bi00155a036 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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