Crystallization (Comment) | Organism |
---|---|
ternary complex of s-GDH with PQQ and methylhydrazine, at 1.5 A resolution. Formation of a covalent PQQ adduct in the active-site. The C5 carbonyl group of the cofactor is the most reactive moiety of PQQ. The binding of the cofactor to s-GDH is predominantly governed by polar interactions. The C2, C7, and C9 carboxyl groups of PQQ form salt bridges with Arg408, Lys377, and Arg406, respectively. The ortho-quinone O4 and O5 atoms are bound by Asn229 and Arg228, respectively. The N6, O7A, and O5 atoms of PQQ are ligands for the active-site calcium ion. The other calcium ligands are provided by the two main chain carbonyl oxygen atoms of Gly-247 and Pro-248 and two watermolecules | Acinetobacter calcoaceticus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
methylhydrazine | competitive inhibitor | Acinetobacter calcoaceticus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acinetobacter calcoaceticus | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
s-GDH | - |
Acinetobacter calcoaceticus |