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1YJL

Reduced Peptidylglycine alpha-Hydroxylating Monooxygenase in a new crystal form

Summary for 1YJL
Entry DOI10.2210/pdb1yjl/pdb
Related1OPM 1PHM 1SDW 1YI9 1YIP 1YJK 3PHM
DescriptorPeptidyl-glycine alpha-amidating monooxygenase (2 entities in total)
Functional Keywordsmonooxygenase, bioactive peptide activation, copper, ascorbate, oxidoreductase
Biological sourceRattus norvegicus (Norway rat)
Cellular locationCytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein: P14925
Total number of polymer chains1
Total formula weight34140.14
Authors
Siebert, X.,Eipper, B.A.,Mains, R.E.,Prigge, S.T.,Blackburn, N.J.,Amzel, L.M. (deposition date: 2005-01-14, release date: 2005-11-15, Last modification date: 2023-08-23)
Primary citationSiebert, 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: 16100265
DOI: 10.1529/biophysj.105.066100
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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