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Literature summary extracted from
- Structure of T4moF, the toluene 4-monooxygenase ferredoxin oxidoreductase (2015), Biochemistry, 54, 5980-5988.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.14.13.236 | structure of toluene 4-monooxygenase ferredoxin oxidoreductase subunit Tmo4F, to 1.6 A resolution. Structure includes ferredoxin, flavin, and NADH binding domains. Close contacts between the C8 methyl group of FAD and [2Fe-2S] ligand Cys36-O represent a pathway for electron transfer between the redox cofactors. Subunit T4moF [2Fe-2S] ligand Cys41 and T4moC [2Fe-2S] ligand His67, along with other electrostatic interactions between the protein partners, form the functional electron transfer interface | Pseudomonas mendocina |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.13.236 | Pseudomonas mendocina | Q03304 | - |
- |
| 1.14.13.236 | Pseudomonas mendocina KR1 | Q03304 | - |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.13.236 | T4moF | - |
Pseudomonas mendocina |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.236 | FAD | - |
Pseudomonas mendocina |  |
| 1.14.13.236 | Ferredoxin | - |
Pseudomonas mendocina |
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Release 2023.1 (January 2023)
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