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Literature summary extracted from
- Structural basis for biomolecular recognition in overlapping binding sites in a diiron enzyme system (2014), Nat. Commun., 5, 5009.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.14.13.236 | high-resolution structures of toluene 4-monooxygenase hydroxylase complexed with its electron transfer protein ferredoxin and comparison with the hydroxylase-effector structure. Ferredoxin or effector protein binding produce different arrangements of conserved residues | Pseudomonas mendocina |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.13.236 | Pseudomonas mendocina | Q00456 | - |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.13.236 | TmoA | - |
Pseudomonas mendocina |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.236 | Ferredoxin | ferredoxin binding leads to rearrangement of a loop about 30 A distal with a tightly matched, hydrogen bonded contact surface that places the [2Fe-2S] and diiron centres in their closest possible approach for electron transfer | Pseudomonas mendocina |
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Release 2023.1 (January 2023)
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