1mmo
From Proteopedia
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|PDB= 1mmo |SIZE=350|CAPTION= <scene name='initialview01'>1mmo</scene>, resolution 2.2Å | |PDB= 1mmo |SIZE=350|CAPTION= <scene name='initialview01'>1mmo</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Methane_monooxygenase Methane monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.25 1.14.13.25] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Methane_monooxygenase Methane monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.25 1.14.13.25] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmo OCA], [http://www.ebi.ac.uk/pdbsum/1mmo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mmo RCSB]</span> | ||
}} | }} | ||
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[[Category: Nordlund, P.]] | [[Category: Nordlund, P.]] | ||
[[Category: Rosenzweig, A C.]] | [[Category: Rosenzweig, A C.]] | ||
| - | [[Category: ACY]] | ||
| - | [[Category: FE]] | ||
[[Category: oxidoreductase (monooxygenase)]] | [[Category: oxidoreductase (monooxygenase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:18:07 2008'' |
Revision as of 19:18, 30 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Methane monooxygenase, with EC number 1.14.13.25 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE
Overview
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.
About this Structure
1MMO is a Protein complex structure of sequences from Methylococcus capsulatus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane., Rosenzweig AC, Frederick CA, Lippard SJ, Nordlund P, Nature. 1993 Dec 9;366(6455):537-43. PMID:8255292
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