1.1.1.45: L-gulonate 3-dehydrogenase
This is an abbreviated version!
For detailed information about L-gulonate 3-dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.45
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1.1.1.45
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protomer
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uronate
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medicine
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drosophila
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lens
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acetoacetate
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dehydrogenation
- 1.1.1.45
-
protomer
-
uronate
- medicine
- drosophila
- lens
- acetoacetate
-
dehydrogenation
Reaction
Synonyms
GDH, GuDH, L-3-aldonate dehydrogenase, L-3-aldonic dehydrogenase, L-3-hydroxyacid dehydrogenase, L-beta-hydroxy-acid-NAD-oxidoreductase, L-beta-hydroxyacid dehydrogenase, L-gulonate 3-dehydrogenase, L-gulonic acid dehydrogenase, More
ECTree
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Subunits
Subunits on EC 1.1.1.45 - L-gulonate 3-dehydrogenase
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dimer
monomer
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X-ray diffraction, natural active protein is presumably a dimer 2 * 36000
additional information
the enzyme possesses two domains, the N-terminal domain with a Rossmann fold and the C-terminal domain with a helical fold. In the N-terminal domain of the NADH-bound structure exist 11 coenzyme-binding residues and two distinct side-chain conformers of coenzyme binding residue Ser124. Subunit dimerization is mediated by numerous intersubunit interactions, including 22 hydrogen bonds and 104 residue pairs of van der Waals interactions, of which those between two cognate C-terminal domains are predominant. Domain and subunit interface structures, structure comparison with the human enzyme, overview
additional information
-
the enzyme possesses two domains, the N-terminal domain with a Rossmann fold and the C-terminal domain with a helical fold. In the N-terminal domain of the NADH-bound structure exist 11 coenzyme-binding residues and two distinct side-chain conformers of coenzyme binding residue Ser124. Subunit dimerization is mediated by numerous intersubunit interactions, including 22 hydrogen bonds and 104 residue pairs of van der Waals interactions, of which those between two cognate C-terminal domains are predominant. Domain and subunit interface structures, structure comparison with the human enzyme, overview