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3fw0
From Proteopedia
(Difference between revisions)
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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)== | ||
<StructureSection load='3fw0' size='340' side='right' caption='[[3fw0]], [[Resolution|resolution]] 2.52Å' scene=''> | <StructureSection load='3fw0' size='340' side='right' caption='[[3fw0]], [[Resolution|resolution]] 2.52Å' scene=''> | ||
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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> | <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> | ||
<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> | <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> | ||
| - | <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]</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=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> |
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<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> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3fw0" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3fw0" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Monooxygenase|Monooxygenase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Eipper, B A]] | [[Category: Eipper, B A]] | ||
[[Category: Mains, R E]] | [[Category: Mains, R E]] | ||
| + | [[Category: Alternative splicing]] | ||
[[Category: Beta propeller]] | [[Category: Beta propeller]] | ||
| + | [[Category: Calcium]] | ||
[[Category: Cleavage on pair of basic residue]] | [[Category: Cleavage on pair of basic residue]] | ||
| + | [[Category: Copper]] | ||
[[Category: Cytoplasmic vesicle]] | [[Category: Cytoplasmic vesicle]] | ||
[[Category: Glycoprotein]] | [[Category: Glycoprotein]] | ||
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[[Category: Transmembrane]] | [[Category: Transmembrane]] | ||
[[Category: Vitamin c]] | [[Category: Vitamin c]] | ||
| + | [[Category: Zinc]] | ||
Revision as of 07:32, 5 December 2018
Structure of Peptidyl-alpha-hydroxyglycine alpha-Amidating Lyase (PAL) bound to alpha-hydroxyhippuric acid (non-peptidic substrate)
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Categories: Buffalo rat | Peptidylamidoglycolate lyase | Amzel, L M | Chufan, E E | De, M | Eipper, B A | Mains, R E | Alternative splicing | Beta propeller | Calcium | Cleavage on pair of basic residue | Copper | Cytoplasmic vesicle | Glycoprotein | Hydroxyhippuric acid | Lyase | Membrane | Mercury | Metal-binding | Monooxygenase | Multifunctional enzyme | Oxidoreductase | Peptide amidation | Phosphoprotein | Substrate | Sulfation | Transmembrane | Vitamin c | Zinc
