The enzyme catalyzes an extradiol cleavage of catechol to form 2-hydroxymuconate semialdehyde with the insertion of two atoms of dioxygen. It is an homo-tetramer and each subunit binds a ferrous ion (PMID10368270).
FE2 308 A IN THE RESTING STATE ENZYME
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Representative PDB structure for FE2 308 A in the resting state enzyme | |
| PDB code | 1mpy | |
| Metal Type in the PDB | iron | |
| Residue name of the metal in the PDB | FE2 | |
| Residue number of the metal in the PDB | 308 | |
| Chain of the metal in the PDB | A | |
| Atom name of the metal in the PDB | FE | |
| Download the coordinates file of the metal site | NOTES ON PDB: In this structure the ferrous ion is coordinated to an acetone molecule that is not a physiological ligand but probably substitutes two water molecules. Circular dichroism (CD), magnetic circular dichroism (MCD) and X-ray absorption spectroscopy (XAS) data on the resting state enzyme support the presence of a five-coordinated Fe2+ site in a square-pyramidal geometry (PMID7756296). | |
| First Coordination Sphere | ||||||
| Ligand Type | Ligand Identity | Residue In MACiE | Donors | Bind Mode | Catalytic? | Notes |
| residue | HIS 153 A | HIS 153 A | NE2 | monodentate | No | - |
| residue | HIS 214 A | HIS 214 A | NE2 | monodentate | No | - |
| residue | GLU 265 A | GLU 265 A | OE1 | monodentate | No | - |
| artifact | ACN 309 A | - | O | monodentate | No | This is not a physiological ligand. In the resting state enzyme it is probably substituted by two water molecules. |