2vd6
From Proteopedia
(Difference between revisions)
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| - | + | ==Human adenylosuccinate lyase in complex with its substrate N6-(1,2- Dicarboxyethyl)-AMP, and its products AMP and fumarate.== | |
| - | + | <StructureSection load='2vd6' size='340' side='right' caption='[[2vd6]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2vd6]] is a 4 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=2VD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VD6 FirstGlance]. <br> | |
| - | ==Disease== | + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2SA:2-[9-(3,4-DIHYDROXY-5-PHOSPHONOOXYMETHYL-TETRAHYDRO-FURAN-2-YL)-9H-PURIN-6-YLAMINO]-SUCCINIC+ACID'>2SA</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br> |
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j91|2j91]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylosuccinate_lyase Adenylosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.2 4.3.2.2] </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=2vd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vd6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vd6 RCSB], [http://www.ebi.ac.uk/pdbsum/2vd6 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Disease == | ||
[[http://www.uniprot.org/uniprot/PUR8_HUMAN PUR8_HUMAN]] Defects in ADSL are the cause of adenylosuccinase deficiency (ADSL deficiency) [MIM:[http://omim.org/entry/103050 103050]]. ADSL deficiency is an autosomal recessive disorder characterized by the accumulation in the body fluids of succinylaminoimidazole-carboxamide riboside (SAICA-riboside) and succinyladenosine (S-Ado). Most children display marked psychomotor delay, often accompanied by epilepsy or autistic features, or both, although some patients may be less profoundly retarded. Occasionally, growth retardation and muscular wasting are also present. | [[http://www.uniprot.org/uniprot/PUR8_HUMAN PUR8_HUMAN]] Defects in ADSL are the cause of adenylosuccinase deficiency (ADSL deficiency) [MIM:[http://omim.org/entry/103050 103050]]. ADSL deficiency is an autosomal recessive disorder characterized by the accumulation in the body fluids of succinylaminoimidazole-carboxamide riboside (SAICA-riboside) and succinyladenosine (S-Ado). Most children display marked psychomotor delay, often accompanied by epilepsy or autistic features, or both, although some patients may be less profoundly retarded. Occasionally, growth retardation and muscular wasting are also present. | ||
| + | == Function == | ||
| - | == | + | == 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/vd/2vd6_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> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Adenylosuccinate lyase]] | [[Category: Adenylosuccinate lyase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 01:28, 1 October 2014
Human adenylosuccinate lyase in complex with its substrate N6-(1,2- Dicarboxyethyl)-AMP, and its products AMP and fumarate.
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Categories: Adenylosuccinate lyase | Homo sapiens | Arrowsmith, C. | Berg, S Van Den. | Berglund, H. | Busam, R. | Collins, R. | Dahlgren, L G. | Edwards, A. | Flodin, S. | Flores, A. | Graslund, S. | Hallberg, B M. | Hammarstrom, M. | Holmberg-Schiavone, L. | Johansson, I. | Kallas, A. | Karlberg, T. | Kotenyova, T. | Lehtio, L. | Moche, M. | Nilsson, M. | Nordlund, P. | Nyman, T. | Ogg, D. | Persson, C. | Sagemark, J. | Sgc, Structural Genomics Consortium. | Stenmark, P. | Sundstrom, M. | Thorsell, A G. | Tresaugues, L. | Weigelt, J. | Welin, M. | Epilepsy | Lyase | Purine biosynthesis | Purine metabolism
