6ala
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of H108A peptidylglycine alpha-hydroxylating monooxygenase (PHM) in complex with citrate== | |
| - | + | <StructureSection load='6ala' size='340' side='right' caption='[[6ala]], [[Resolution|resolution]] 2.59Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6ala]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ALA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ALA 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=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wja|5wja]], [[5wkw|5wkw]], [[5wm0|5wm0]]</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=6ala FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ala OCA], [http://pdbe.org/6ala PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ala RCSB], [http://www.ebi.ac.uk/pdbsum/6ala PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ala 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: Amzel, L M]] | ||
| + | [[Category: Gabelli, S B]] | ||
| + | [[Category: Maheshwari, S]] | ||
| + | [[Category: Rudzka, K]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Peptidylglycine 2-hydroxylase]] | ||
| + | [[Category: Peptidylglycine monooxygenase]] | ||
| + | [[Category: Phm]] | ||
Revision as of 07:33, 18 July 2018
Crystal structure of H108A peptidylglycine alpha-hydroxylating monooxygenase (PHM) in complex with citrate
| |||||||||||
