Cloned (Comment) | Organism |
---|---|
- |
Thermotoga maritima |
Crystallization (Comment) | Organism |
---|---|
mutant H53D, in complex with the methyl donor, CH2H4 folate. The substrate-binding loop can be stabilized in two conformations and this affects the binding of the molecules at the substrate binding site. The isoalloxazine (flavin) ring of FAD binds in a big pocket that tolerates large movements of the isoalloxazine ring. The isoalloxazine ring is able to rotate in the binding pocket and utilize same face of the ring to bind to substrate and cofactors | Thermotoga maritima |
Protein Variants | Comment | Organism |
---|---|---|
H53D | residue H53 is involved in folate binding. Crystal structures of the H53D-FAD and H53D-FAD-dUMP complexes | Thermotoga maritima |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermotoga maritima | Q9WYT0 | - |
- |
Thermotoga maritima ATCC 43589 | Q9WYT0 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
FDTS | - |
Thermotoga maritima |