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6e9p
From Proteopedia
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==Crystal structure of tryptophan synthase from M. tuberculosis - open form with BRD0059 bound== | ==Crystal structure of tryptophan synthase from M. tuberculosis - open form with BRD0059 bound== | ||
| - | <StructureSection load='6e9p' size='340' side='right' caption='[[6e9p]], [[Resolution|resolution]] 2.57Å' scene=''> | + | <StructureSection load='6e9p' size='340' side='right'caption='[[6e9p]], [[Resolution|resolution]] 2.57Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6e9p]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E9P OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[6e9p]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E9P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6E9P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=HDJ:(2R,3S,4R)-3-(2,6-difluoro-4-methyl[1,1-biphenyl]-4-yl)-4-(fluoromethyl)azetidine-2-carbonitrile'>HDJ</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=HDJ:(2R,3S,4R)-3-(2,6-difluoro-4-methyl[1,1-biphenyl]-4-yl)-4-(fluoromethyl)azetidine-2-carbonitrile'>HDJ</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </span></td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6e9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e9p OCA], [http://pdbe.org/6e9p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e9p RCSB], [http://www.ebi.ac.uk/pdbsum/6e9p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e9p ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/TRPA_MYCTU TRPA_MYCTU]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [[http://www.uniprot.org/uniprot/TRPB_MYCTU TRPB_MYCTU]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine (By similarity). | [[http://www.uniprot.org/uniprot/TRPA_MYCTU TRPA_MYCTU]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [[http://www.uniprot.org/uniprot/TRPB_MYCTU TRPB_MYCTU]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine (By similarity). | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]] | ||
| + | *[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Tryptophan synthase]] | [[Category: Tryptophan synthase]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
Revision as of 09:10, 11 November 2020
Crystal structure of tryptophan synthase from M. tuberculosis - open form with BRD0059 bound
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Categories: Large Structures | Tryptophan synthase | Structural genomic | Chang, C | Jedrzejczak, R | Joachimiak, A | Maltseva, N I | McCarren, P | Michalska, K | Nag, P P | Satchell, K | Allostery | Amino acid biosynthesis | Csgid | Heterotetramer | Lyase | Lyase-lyase inhibitor complex | Plp | Substrate channeling
