Literature summary for 1.1.1.12 extracted from

Tiwari, M.; Lee, J.K.
Molecular modeling studies of L-arabinitol 4-dehydrogenase of Hypocrea jecorina: its binding interactions with substrate and cofactor (2010), J. Mol. Graph. Model., 28, 707-713.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
docking study with the substrate L-arabinitol, Zn2+ and NAD+ reveals a catalytic Zn2+ binding domain involving residues Cys66, His91, Glu92 and Glu176, and a cofactor NAD+ binding domain involving residues Gly202, ILeu204, Gly205, Cys273, Arg229 and Val298, with strong hydrogen bonding contacts with the substrate and cofactor	Trichoderma reesei

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	catalytic Zn2+ binding domain involving residues Cys66, His91, Glu92 and Glu176, molecular docking studies	Trichoderma reesei

Organism

Organism	UniProt	Comment	Textmining
Trichoderma reesei	Q96V44	-	-

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	cofactor NAD+ binding domain involving residues Gly202, ILeu204, Gly205, Cys273, Arg229 and Val298, molecular docking studies	Trichoderma reesei

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Release 2023.1 (January 2023)