1phm | pdb_00001phm

PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) FROM RAT

spinqualitylabelsall models 1phm, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1phm is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: AZI, CU, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AMD_RAT Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also Monooxygenase 3D structures

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