1MMO
CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE
Summary for 1MMO
| Entry DOI | 10.2210/pdb1mmo/pdb |
| Descriptor | METHANE MONOOXYGENASE HYDROLASE (BETA CHAIN), METHANE MONOOXYGENASE HYDROLASE (ALPHA CHAIN), METHANE MONOOXYGENASE HYDROLASE (GAMMA CHAIN), ... (6 entities in total) |
| Functional Keywords | oxidoreductase (monooxygenase) |
| Biological source | Methylococcus capsulatus More |
| Total number of polymer chains | 6 |
| Total formula weight | 245693.23 |
| Authors | Rosenzweig, A.C.,Frederick, C.A.,Lippard, S.J.,Nordlund, P. (deposition date: 1994-02-22, release date: 1995-02-27, Last modification date: 2024-02-14) |
| Primary citation | Rosenzweig, A.C.,Frederick, C.A.,Lippard, S.J.,Nordlund, P. Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. Nature, 366:537-543, 1993 Cited by PubMed Abstract: The 2.2 A crystal structure of the 251K alpha 2 beta 2 gamma 2 dimeric hydroxylase protein of methane monooxygenase from Methylococcus capsulatus (Bath) reveals the geometry of the catalytic di-iron core. The two iron atoms are bridged by exogenous hydroxide and acetate ligands and further coordinated by four glutamate residues, two histidine residues and a water molecule. The dinuclear iron centre lies in a hydrophobic active-site cavity for binding methane. An extended canyon runs between alpha beta pairs, which have many long alpha-helices, for possible docking of the reductase and coupling proteins required for catalysis. PubMed: 8255292DOI: 10.1038/366537a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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