EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.9.1 | to 1.44 A resolution. The N-terminal domain has a beta-propeller fold and binds one pyrroloquinoline quinone cofactor and one calcium ion in the active site. A tetrahydrofuran-2-carboxylic acid molecule is present in the substrate-binding cleft. The C-terminal domain is an -helical type I cytochrome c with His608 and Met647 as heme-iron ligands. An unusual disulfide bond between two adjacent cysteines bridges the redox centers. It appears essential for electron transfer. A water channel delineates a possible pathway for proton transfer from the active site to the solvent | Comamonas testosteroni |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.9.1 | Comamonas testosteroni | Q46444 | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.5.5 | alcohol dehydrogenase | - |
- |