Literature summary for 1.1.99.35 extracted from

Oubrie, A.; Rozeboom, H.J.; Kalk, K.H.; Duine, J.A.; Dijkstra, B.W.
The 1.7 A crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat (1999), J. Mol. Biol., 289, 319-333.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
at 1.72 A resolution. The s-GDH monomer has a beta-propeller fold consisting of six four-stranded anti-parallel beta-sheets aligned around a pseudo 6-fold symmetry axis. The enzyme binds three calcium ions per monomer, two of which are located in the dimer interface. The third is bound in the putative active site, where it may bind and functionalize the pyrroloquinoline quinone cofactor	Acinetobacter calcoaceticus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	the enzyme binds three calcium ions per monomer, two of which are located in the dimer interface, crystallization data	Acinetobacter calcoaceticus

Organism

Organism	UniProt	Comment	Textmining
Acinetobacter calcoaceticus	P13650	-	-

Cofactor

Cofactor	Comment	Organism	Structure
pyrroloquinoline quinone	crystallization data	Acinetobacter calcoaceticus

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Release 2023.1 (January 2023)