6ao6
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of H108A peptidylglycine alpha-hydroxylating monooxygenase (PHM)== | |
| - | + | <StructureSection load='6ao6' size='340' side='right' caption='[[6ao6]], [[Resolution|resolution]] 2.98Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6ao6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AO6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AO6 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </span></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=6ao6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ao6 OCA], [http://pdbe.org/6ao6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ao6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ao6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ao6 ProSAT]</span></td></tr> | ||
| + | </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: Peptidylglycine monooxygenase]] | ||
| + | [[Category: Amzel, L M]] | ||
| + | [[Category: Gabelli, S B]] | ||
[[Category: Maheshwari, S]] | [[Category: Maheshwari, S]] | ||
[[Category: Rudzka, K]] | [[Category: Rudzka, K]] | ||
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | [[Category: | + | [[Category: Peptidylglycine 2-hydroxylase]] |
| + | [[Category: Phm]] | ||
Revision as of 07:33, 18 July 2018
Crystal structure of H108A peptidylglycine alpha-hydroxylating monooxygenase (PHM)
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