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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>
= <Biological unit>

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PDB ID3mic  sequence information (FASTA format)   
RELATED PDB ID1phm, 3mib, 3mid, 3mie, 3mif, 3mig, 3mih, 3mlj, 3mlk, 3mll
DescriptorPeptidyl-glycine alpha-amidating monooxygenase (E.C.1.14.17.3)
TitleOxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound azide obtained by co-crystallization
Functional KeywordsOXIDOREDUCTASE, MONOOXYGENASE, BIOACTIVE PEPTIDE ACTIVATION, ASCORBATE
Biological sourceRattus norvegicus (rat)
Cellular location [UNP - P14925] Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein
Organ source [UNP - P14925] Heart atrium
[UNP - P14925] Pituitary
[UNP - P14925] Liver
Total number of polymer chains1
Total molecular weight35600.4 (the details in Structural Details Page)
AuthorsChufan, E.E. , Eipper, B.A. , Mains, R.E. , Amzel, L.M. (deposition date : 2010-04-10, release date : 2010-11-24)
Primary citationChufan, 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.(PubMed : 20958070)  (DOI: 10.1021/ja103117r)
Experimental methodX-RAY DIFFRACTION ( 2.42[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P14925 ) , eF-site , KEGG ( EC 1.14.17.3 ) , PISA