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Literature summary extracted from
- The mechanism of aconitase:1.8 A resolution crystal structure of the S642A:citrate complex (1999), Protein Sci., 8, 2655-2662.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.2.1.3 | 1.8 A resolution crystal structure of the S642A:citrate complex of mitochondrial aconitase | Sus scrofa |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 4.2.1.3 | mitochondrion | - |
Sus scrofa | 5739 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.3 | Iron | in the S642A:citrate complex citrate is directly coordinated to Fe4 of the [4Fe-4S] cluster via Cbeta carboxyl and hydroxyl oxygen atoms | Sus scrofa |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.3 | Sus scrofa | P16276 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.3 | additional information | the mechanism requires that the intermediate product cis-aconitate, flip over by 180° about the Calpha-Cbeta double bond | Sus scrofa | ? | - |
? | |
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