5txr: Difference between revisions
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==Structure of ALAS from S. cerevisiae non-covalently bound to PLP cofactor== | |||
<StructureSection load='5txr' size='340' side='right' caption='[[5txr]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5txr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TXR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TXR FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | |||
[[Category: | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5txt|5txt]]</td></tr> | ||
[[Category: Kardon, J | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5-aminolevulinate_synthase 5-aminolevulinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.37 2.3.1.37] </span></td></tr> | ||
[[Category: Sauer, R | <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=5txr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5txr OCA], [http://pdbe.org/5txr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5txr RCSB], [http://www.ebi.ac.uk/pdbsum/5txr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5txr ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: | == Function == | ||
[[Category: | [[http://www.uniprot.org/uniprot/HEM1_YEAST HEM1_YEAST]] Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis.<ref>PMID:6381051</ref> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: 5-aminolevulinate synthase]] | |||
[[Category: Baker, T A]] | |||
[[Category: Brown, B L]] | |||
[[Category: Grant, R A]] | |||
[[Category: Kardon, J R]] | |||
[[Category: Sauer, R T]] | |||
[[Category: 5-aminolevulinic acid]] | |||
[[Category: Heme biosynthesis]] | |||
[[Category: Pyridoxal 5-phosphate]] | |||
[[Category: Transferase]] | |||
Revision as of 06:30, 28 March 2018
Structure of ALAS from S. cerevisiae non-covalently bound to PLP cofactor
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