1SDW
Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase with bound peptide and dioxygen
Summary for 1SDW
| Entry DOI | 10.2210/pdb1sdw/pdb |
| Related | 1opm 1phm 3phm |
| Descriptor | Peptidyl-glycine alpha-amidating monooxygenase, COPPER (II) ION, NICKEL (II) ION, ... (7 entities in total) |
| Functional Keywords | beta jelly-roll, oxidoreductase |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein: P14925 |
| Total number of polymer chains | 1 |
| Total formula weight | 37506.85 |
| Authors | Prigge, S.T.,Eipper, B.A.,Mains, R.E.,Amzel, L.M. (deposition date: 2004-02-14, release date: 2004-05-11, Last modification date: 2024-10-30) |
| Primary citation | Prigge, S.T.,Eipper, B.A.,Mains, R.E.,Amzel, L.M. Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex. Science, 304:864-867, 2004 Cited by PubMed Abstract: Copper active sites play a major role in enzymatic activation of dioxygen. We trapped the copper-dioxygen complex in the enzyme peptidylglycine-alphahydroxylating monooxygenase (PHM) by freezing protein crystals that had been soaked with a slow substrate and ascorbate in the presence of oxygen. The x-ray crystal structure of this precatalytic complex, determined to 1.85-angstrom resolution, shows that oxygen binds to one of the coppers in the enzyme with an end-on geometry. Given this structure, it is likely that dioxygen is directly involved in the electron transfer and hydrogen abstraction steps of the PHM reaction. These insights may apply to other copper oxygen-activating enzymes, such as dopamine beta-monooxygenase, and to the design of biomimetic complexes. PubMed: 15131304DOI: 10.1126/science.1094583 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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