3fw0

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==Structure of Peptidyl-alpha-hydroxyglycine alpha-Amidating Lyase (PAL) bound to alpha-hydroxyhippuric acid (non-peptidic substrate)==
==Structure of Peptidyl-alpha-hydroxyglycine alpha-Amidating Lyase (PAL) bound to alpha-hydroxyhippuric acid (non-peptidic substrate)==
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<StructureSection load='3fw0' size='340' side='right' caption='[[3fw0]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
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<StructureSection load='3fw0' size='340' side='right'caption='[[3fw0]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3fw0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FW0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3fw0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FW0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=HH3:(2S)-HYDROXY[(PHENYLCARBONYL)AMINO]ETHANOIC+ACID'>HH3</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.52&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fvz|3fvz]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=HH3:(2S)-HYDROXY[(PHENYLCARBONYL)AMINO]ETHANOIC+ACID'>HH3</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fw0 OCA], [https://pdbe.org/3fw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fw0 RCSB], [https://www.ebi.ac.uk/pdbsum/3fw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fw0 ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylamidoglycolate_lyase Peptidylamidoglycolate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.5 4.3.2.5] </span></td></tr>
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<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=3fw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fw0 OCA], [http://pdbe.org/3fw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fw0 RCSB], [http://www.ebi.ac.uk/pdbsum/3fw0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fw0 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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.
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[https://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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fw/3fw0_consurf.spt"</scriptWhenChecked>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fw/3fw0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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==See Also==
==See Also==
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*[[Monooxygenase|Monooxygenase]]
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*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
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[[Category: Large Structures]]
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[[Category: Peptidylamidoglycolate lyase]]
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[[Category: Rattus norvegicus]]
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[[Category: Amzel, L M]]
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[[Category: Amzel LM]]
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[[Category: Chufan, E E]]
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[[Category: Chufan EE]]
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[[Category: De, M]]
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[[Category: De M]]
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[[Category: Eipper, B A]]
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[[Category: Eipper BA]]
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[[Category: Mains, R E]]
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[[Category: Mains RE]]
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[[Category: Alternative splicing]]
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[[Category: Beta propeller]]
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[[Category: Calcium]]
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[[Category: Cleavage on pair of basic residue]]
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[[Category: Copper]]
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[[Category: Cytoplasmic vesicle]]
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[[Category: Glycoprotein]]
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[[Category: Hydroxyhippuric acid]]
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[[Category: Lyase]]
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[[Category: Membrane]]
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[[Category: Mercury]]
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[[Category: Metal-binding]]
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[[Category: Monooxygenase]]
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[[Category: Multifunctional enzyme]]
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[[Category: Oxidoreductase]]
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[[Category: Peptide amidation]]
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[[Category: Phosphoprotein]]
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[[Category: Substrate]]
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[[Category: Sulfation]]
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[[Category: Transmembrane]]
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[[Category: Vitamin c]]
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[[Category: Zinc]]
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Current revision

Structure of Peptidyl-alpha-hydroxyglycine alpha-Amidating Lyase (PAL) bound to alpha-hydroxyhippuric acid (non-peptidic substrate)

PDB ID 3fw0

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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