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Structure paper

TitleThe catalytic copper of Peptidylglycine alpha-Hydroxylating Monooxygenase also plays a critical structural role.
Journal, issue, pagesBiophys. J., Vol. 89, Page 3312-3319, Year 2005
Publish dateJan 11, 2005 (structure data deposition date)
AuthorsSiebert, X. / Eipper, B.A. / Mains, R.E. / Prigge, S.T. / Blackburn, N.J. / Amzel, L.M.
External linksBiophys. J. / PubMed:16100265
MethodsX-ray diffraction
Resolution1.7 - 2.4 Å
Structure data

PDB-1yi9:
Crystal Structure Analysis of the oxidized form of the M314I mutant of Peptidylglycine alpha-Hydroxylating Monooxygenase
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-1yip:
Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1yjk:
Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1yjl:
Reduced Peptidylglycine alpha-Hydroxylating Monooxygenase in a new crystal form
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • rattus norvegicus (Norway rat)
KeywordsOXIDOREDUCTASE / MONOOXYGENASE / BIOACTIVE PEPTIDE ACTIVATION / ASCORBATE / COPPER

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