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 | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | catalytic Zn2+ binding domain involving residues Cys66, His91, Glu92 and Glu176, molecular docking studies | Trichoderma reesei |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Trichoderma reesei | Q96V44 | - |
- |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | cofactor NAD+ binding domain involving residues Gly202, ILeu204, Gly205, Cys273, Arg229 and Val298, molecular docking studies | Trichoderma reesei |