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). 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):
This entry contains 1 unique UniProt protein: