Crystallization (Comment) | Organism |
---|---|
to 1.88 A resolution, space group P41212. Spherical protein, consists of four domains with a funnel-like cavity that leads to the freely accessible metal-ion redox center. The bis(molybdopterin guanine dinucleotide) molybdenum cofactor of the single chain protein has the molybdenum ion bound to the cis-dithiolene group of only one molybdopterin guanine dinucleotide molecule. Three additional ligands, two oxo groups and the oxygen of a serine side-chain, are bound to the molybdenum ion. The second molybdopterin system is not part of the ligand sphere of the metal center | Rhodobacter capsulatus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Molybdenum | the bis-molybdopterin guanine dinucleotide cofactor of the single chain protein has the molybdenum ion bound to the cis-dithiolene group of only one molybdopterin guanine dinucleotide molecule. Three additional ligands, two oxo groups and the oxygen of a serine side-chain, are bound to the molybdenum ion. The second molybdopterin system is not part of the ligand sphere of the metal center | Rhodobacter capsulatus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodobacter capsulatus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Rhodobacter capsulatus |
Subunits | Comment | Organism |
---|---|---|
? | x * 85,033, calculated | Rhodobacter capsulatus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
bis(molybdopterin guanine dinucleotide)molybdenum cofactor | the bis-molybdopterin guanine dinucleotide cofactor of the single chain protein has the molybdenum ion bound to the cis-dithiolene group of only one molybdopterin guanine dinucleotide molecule. Three additional ligands, two oxo groups and the oxygen of a serine side-chain, are bound to the molybdenum ion. The second molybdopterin system is not part of the ligand sphere of the metal center | Rhodobacter capsulatus |