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Literature summary extracted from

  • White, S.; Boyd, G.; Mathews, F.S.; Xia, Z.X.; Dai, W.W.; Zhang, Y.F.; Davidson, V.L.
    The active site structure of the calcium-containing quinoprotein methanol dehydrogenase (1993), Biochemistry, 32, 12955-12958.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.2.7 Ca2+ Ca2+ is six-coordinated with bonds to 05, N6, and carboxyl oxygen 07A of PQQ, the two carboxyl oxygen atoms of Glu171, and the side-chain oxygen of Asn255, binding structure, overview Methylophilus sp.

Organism

EC Number Organism UniProt Comment Textmining
1.1.2.7 Methylophilus sp.
-
-
-
1.1.2.7 Methylophilus sp. W3A1
-
-
-

Subunits

EC Number Subunits Comment Organism
1.1.2.7 tetramer heterotetramer, structure analysis and modelling, overview Methylophilus sp.

Synonyms

EC Number Synonyms Comment Organism
1.1.2.7 MEDH
-
 Methylophilus sp.
1.1.2.7 methanol dehydrogenase
-
 Methylophilus sp.
1.1.5.5 bacterial methanol dehydrogenase
-
-
1.1.5.5 calcium-containing quinoprotein methanol dehydrogenase
-
-
1.1.5.5 MEDH
-
-

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.2.7 pyrroloquinoline quinone PQQ, serves as the redox cofactor in bacterial MEDH, PQQ is located in a central channel of the disk-shaped protein, and is sandwiched between a Trp side chain and a very unusual vicinal disulfide, binding structure, overview Methylophilus sp.