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2h5g
From Proteopedia
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==Crystal structure of human pyrroline-5-carboxylate synthetase== | ==Crystal structure of human pyrroline-5-carboxylate synthetase== | ||
| - | <StructureSection load='2h5g' size='340' side='right' caption='[[2h5g]], [[Resolution|resolution]] 2.25Å' scene=''> | + | <StructureSection load='2h5g' size='340' side='right'caption='[[2h5g]], [[Resolution|resolution]] 2.25Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2h5g]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2h5g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H5G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H5G FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALDH18A1 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALDH18A1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate-5-semialdehyde_dehydrogenase Glutamate-5-semialdehyde dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.41 1.2.1.41] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h5g OCA], [https://pdbe.org/2h5g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h5g RCSB], [https://www.ebi.ac.uk/pdbsum/2h5g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h5g ProSAT]</span></td></tr> |
| - | <table> | + | </table> |
== Disease == | == Disease == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/P5CS_HUMAN P5CS_HUMAN]] Defects in ALDH18A1 are the cause of cutis laxa, autosomal recessive, type 3A (ARCL3A) [MIM:[https://omim.org/entry/219150 219150]]. A syndrome characterized by facial dysmorphism with a progeroid appearance, large and late-closing fontanel, cutis laxa, joint hyperlaxity, athetoid movements and hyperreflexia, pre- and postnatal growth retardation, intellectual deficit, developmental delay, and ophthalmologic abnormalities.<ref>PMID:11092761</ref> <ref>PMID:18478038</ref> |
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/P5CS_HUMAN P5CS_HUMAN]] Bifunctional enzyme that converts glutamate to glutamate 5-semialdehyde, an intermediate in the biosynthesis of proline, ornithine and arginine.<ref>PMID:10037775</ref> <ref>PMID:11092761</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h5/2h5g_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h5/2h5g_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> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2h5g ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Glutamate-5-semialdehyde dehydrogenase]] | [[Category: Glutamate-5-semialdehyde dehydrogenase]] | ||
| - | [[Category: | + | [[Category: Human]] |
| - | [[Category: Arrowsmith, C | + | [[Category: Large Structures]] |
| - | [[Category: Berridge, G | + | [[Category: Arrowsmith, C]] |
| - | [[Category: Bray, J | + | [[Category: Berridge, G]] |
| - | [[Category: Edwards, A | + | [[Category: Bray, J]] |
| - | [[Category: Gileadi, O | + | [[Category: Edwards, A]] |
| - | [[Category: Gorrec, F | + | [[Category: Gileadi, O]] |
| - | [[Category: Hozjan, V | + | [[Category: Gorrec, F]] |
| - | [[Category: Kavanagh, K | + | [[Category: Hozjan, V]] |
| - | [[Category: Oppermann, U | + | [[Category: Kavanagh, K]] |
| - | [[Category: Papagrigoriou, E | + | [[Category: Oppermann, U]] |
| - | [[Category: | + | [[Category: Papagrigoriou, E]] |
| - | [[Category: Shafqat, N | + | [[Category: Structural genomic]] |
| - | [[Category: Smee, C | + | [[Category: Shafqat, N]] |
| - | [[Category: Sundstrom, M | + | [[Category: Smee, C]] |
| - | [[Category: Turnbull, A P | + | [[Category: Sundstrom, M]] |
| - | [[Category: Weigelt, J | + | [[Category: Turnbull, A P]] |
| + | [[Category: Weigelt, J]] | ||
[[Category: Dehydrogenase]] | [[Category: Dehydrogenase]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Sgc]] | [[Category: Sgc]] | ||
| - | [[Category: Structural genomic]] | ||
| - | [[Category: Structural genomics consortium]] | ||
Current revision
Crystal structure of human pyrroline-5-carboxylate synthetase
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Categories: Glutamate-5-semialdehyde dehydrogenase | Human | Large Structures | Arrowsmith, C | Berridge, G | Bray, J | Edwards, A | Gileadi, O | Gorrec, F | Hozjan, V | Kavanagh, K | Oppermann, U | Papagrigoriou, E | Structural genomic | Shafqat, N | Smee, C | Sundstrom, M | Turnbull, A P | Weigelt, J | Dehydrogenase | Oxidoreductase | Sgc
