3MIC
Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound azide obtained by co-crystallization
Summary for 3MIC
Entry DOI | 10.2210/pdb3mic/pdb |
Related | 1PHM 3MIB 3MID 3MIE 3MIF 3MIG 3MIH 3MLJ 3MLK 3MLL |
Descriptor | Peptidyl-glycine alpha-amidating monooxygenase, COPPER (II) ION, NICKEL (II) ION, ... (7 entities in total) |
Functional Keywords | oxidoreductase, monooxygenase, bioactive peptide activation, ascorbate |
Biological source | Rattus norvegicus (rat) |
Cellular location | Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein: P14925 |
Total number of polymer chains | 1 |
Total formula weight | 35600.22 |
Authors | Chufan, E.E.,Eipper, B.A.,Mains, R.E.,Amzel, L.M. (deposition date: 2010-04-10, release date: 2010-11-24, Last modification date: 2023-09-06) |
Primary citation | Chufan, E.E.,Prigge, S.T.,Siebert, X.,Eipper, B.A.,Mains, R.E.,Amzel, L.M. Differential Reactivity Between the Two Copper Sites of Peptidylglycine alpha-Hydroxylating Monooxygenase (PHM) J.Am.Chem.Soc., 132:15565-15572, 2010 Cited by PubMed: 20958070DOI: 10.1021/ja103117r PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.42 Å) |
Structure validation
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