2h5g
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal structure of human pyrroline-5-carboxylate synthetase== | |
- | + | <StructureSection load='2h5g' size='340' side='right' caption='[[2h5g]], [[Resolution|resolution]] 2.25Å' scene=''> | |
- | + | == Structural highlights == | |
- | ==Disease== | + | <table><tr><td colspan='2'>[[2h5g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H5G FirstGlance]. <br> |
- | [[http://www.uniprot.org/uniprot/P5CS_HUMAN P5CS_HUMAN]] Defects in ALDH18A1 are the cause of cutis laxa, autosomal recessive, type 3A (ARCL3A) [MIM:[http://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> | + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> |
- | + | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |
- | ==Function== | + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALDH18A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> |
- | [[http://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> | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate-5-semialdehyde_dehydrogenase Glutamate-5-semialdehyde dehydrogenase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h5g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h5g RCSB], [http://www.ebi.ac.uk/pdbsum/2h5g PDBsum]</span></td></tr> | |
- | == | + | <table> |
- | [[ | + | == Disease == |
- | + | [[http://www.uniprot.org/uniprot/P5CS_HUMAN P5CS_HUMAN]] Defects in ALDH18A1 are the cause of cutis laxa, autosomal recessive, type 3A (ARCL3A) [MIM:[http://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 == |
- | <references | + | [[http://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 == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <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> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Glutamate-5-semialdehyde dehydrogenase]] | [[Category: Glutamate-5-semialdehyde dehydrogenase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] |
Revision as of 09:29, 30 September 2014
Crystal structure of human pyrroline-5-carboxylate synthetase
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Categories: Glutamate-5-semialdehyde dehydrogenase | Homo sapiens | Arrowsmith, C. | Berridge, G. | Bray, J. | Edwards, A. | Gileadi, O. | Gorrec, F. | Hozjan, V. | Kavanagh, K. | Oppermann, U. | Papagrigoriou, E. | SGC, Structural Genomics Consortium. | Shafqat, N. | Smee, C. | Sundstrom, M. | Turnbull, A P. | Weigelt, J. | Dehydrogenase | Oxidoreductase | Sgc | Structural genomic | Structural genomics consortium