1PHM
PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) FROM RAT
Summary for 1PHM
| Entry DOI | 10.2210/pdb1phm/pdb |
| Descriptor | PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE, COPPER (II) ION, AZIDE ION, ... (5 entities in total) |
| Functional Keywords | monooxygenase, bioactive peptide activation, 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 | 35178.67 |
| Authors | Prigge, S.T.,Amzel, L.M. (deposition date: 1997-10-10, release date: 1998-11-11, Last modification date: 2011-07-13) |
| Primary citation | Prigge, S.T.,Kolhekar, A.S.,Eipper, B.A.,Mains, R.E.,Amzel, L.M. Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase. Science, 278:1300-1305, 1997 Cited by PubMed: 9360928DOI: 10.1126/science.278.5341.1300 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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