5wm0: Difference between revisions
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==Crystal structure of apo wild type peptidylglycine alpha-hydroxylating monooxygenase (PHM) soaked with peptide (peptide not observed)== | |||
<StructureSection load='5wm0' size='340' side='right' caption='[[5wm0]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5wm0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WM0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WM0 FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wm0 OCA], [http://pdbe.org/5wm0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wm0 RCSB], [http://www.ebi.ac.uk/pdbsum/5wm0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wm0 ProSAT]</span></td></tr> | |||
[[Category: | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/AMD_RAT 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. | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Amzel, L M]] | |||
[[Category: Gabelli, S B]] | |||
[[Category: Maheshwari, S]] | |||
[[Category: Rudzka, K]] | [[Category: Rudzka, K]] | ||
[[Category: | [[Category: Metal binding protein]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: | [[Category: Peptidylglycine 2-hydroxylase]] | ||
[[Category: Peptidylglycine monooxygenase]] | |||
[[Category: Phm]] | |||
Revision as of 10:28, 18 July 2018
Crystal structure of apo wild type peptidylglycine alpha-hydroxylating monooxygenase (PHM) soaked with peptide (peptide not observed)Crystal structure of apo wild type peptidylglycine alpha-hydroxylating monooxygenase (PHM) soaked with peptide (peptide not observed)
Structural highlights
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. |
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