1YIP
Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form
Summary for 1YIP
Entry DOI | 10.2210/pdb1yip/pdb |
Related | 1OPM 1PHM 1SDW 1YI9 3PHM |
Descriptor | Peptidyl-glycine alpha-amidating monooxygenase, COPPER (II) ION (3 entities in total) |
Functional Keywords | monooxygenase, bioactive peptide activation, copper, ascorbate, 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 | 34801.85 |
Authors | Siebert, X.,Eipper, B.A.,Mains, R.E.,Prigge, S.T.,Blackburn, N.J.,Amzel, L.M. (deposition date: 2005-01-12, release date: 2005-11-15, Last modification date: 2023-08-23) |
Primary citation | Siebert, X.,Eipper, B.A.,Mains, R.E.,Prigge, S.T.,Blackburn, N.J.,Amzel, L.M. The Catalytic Copper of Peptidylglycine alpha-Hydroxylating Monooxygenase also Plays a Critical Structural Role. Biophys.J., 89:3312-3319, 2005 Cited by PubMed: 16100265DOI: 10.1529/biophysj.105.066100 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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