Literature summary extracted from
Martins, B.M.; Dobbek, H.; Cinkaya, I.; Buckel, W.; Messerschmidt, A.
Crystal structure of 4-hydroxybutyryl-CoA dehydratase: Radical catalysis involving a [4Fe-4S] cluster and flavin (2004), Proc. Natl. Acad. Sci. USA, 101, 15645-15649.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.2.1.120 |
to 1.6 A resolution. A [4Fe-4S]2+ cluster, coordinated by three cysteine and one histidine residues, is located 7 A from the Re-side of a flavin adenine dinucleotide moiety. The substrate can be bound between the [4Fe-4S]2+ cluster and the FAD with both cofactors contributing to its radical activation and catalytic conversio |
Clostridium aminobutyricum |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.1.120 |
Clostridium aminobutyricum |
P55792 |
- |
- |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
4.2.1.120 |
4Fe-4S-center |
a [4Fe-4S]2+ cluster, coordinated by three cysteine and one histidine residues, is located 7 A from the Re-side of a flavin adenine dinucleotide moiety |
Clostridium aminobutyricum |
|
4.2.1.120 |
FAD |
a [4Fe-4S]2+cluster, coordinated by three cysteine and one histidine residues, is located 7 A from the Re-side of a flavin adenine dinucleotide moiety |
Clostridium aminobutyricum |
|