1sdw Summary

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Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase with bound peptide and dioxygen

The structure was published by Prigge, S.T., Eipper, B.A., Mains, R.E., and Amzel, L.M., in 2004 in a paper entitled "Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.85 Å and deposited in 2004.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of Peptidyl-glycine alpha-amidating monooxygenase. This molecule has the UniProt identifier P14925 (AMD_RAT)search. The sample contained 314 residues which is < 90% of the natural sequence. Out of 314 residues 312 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Peptidyl-glycine alpha-amidating monooxygenase P14925 (43-356) (AMD_RAT)search Rattus norvegicussearch < 90% 314 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P14925 (43 - 356) Peptidyl-glycine alpha-amidating monooxygenase Rattus norvegicus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Peptidylglycine alpha-hydroxylating monooxygenase, PHMsearch Jelly Rollssearch Copper type II ascorbate-dependent monooxygenase, N-terminal domainsearch, Copper type II ascorbate-dependent monooxygenase, C-terminal domainsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P14925) oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygensearch copper ion bindingsearch monooxygenase activitysearch catalytic activitysearch peptidylglycine monooxygenase activitysearch membranesearch oxidation-reduction processsearch peptide metabolic processsearch

Chain InterPro annotation
A Copper type II, ascorbate-dependent monooxygenase, N-terminalsearch Peptidyl-glycine alpha-amidating monooxygenasesearch PHM/PNGase F domainsearch Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-2 conserved sitesearch Copper type II, ascorbate-dependent monooxygenase-like, C-terminalsearch Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-1 conserved sitesearch