5n82
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of an engineered TycA variant in complex with an beta-Phe-AMP analog== | |
- | + | <StructureSection load='5n82' size='340' side='right' caption='[[5n82]], [[Resolution|resolution]] 1.71Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5n82]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N82 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N82 FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8PZ:[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+~{N}-[(3~{S})-3-azanyl-3-phenyl-propanoyl]sulfamate'>8PZ</scene>, <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
- | [[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phenylalanine_racemase_(ATP-hydrolyzing) Phenylalanine racemase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.11 5.1.1.11] </span></td></tr> |
+ | <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=5n82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n82 OCA], [http://pdbe.org/5n82 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n82 RCSB], [http://www.ebi.ac.uk/pdbsum/5n82 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n82 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/TYCA_BREPA TYCA_BREPA]] In the first step of peptide synthesis this enzyme activates phenylalanine and racemizes it to the D-isomer. | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Fercher, D]] | [[Category: Fercher, D]] | ||
- | [[Category: | + | [[Category: Hansen, D L]] |
[[Category: Hilvert, D]] | [[Category: Hilvert, D]] | ||
[[Category: Kries, H]] | [[Category: Kries, H]] | ||
- | [[Category: | + | [[Category: Mori, T]] |
- | [[Category: Niquille, D | + | [[Category: Niquille, D L]] |
+ | [[Category: Adenylation domain]] | ||
+ | [[Category: Ligase]] | ||
+ | [[Category: Nonribosomal peptide synthetase]] |
Revision as of 06:54, 13 December 2017
Crystal structure of an engineered TycA variant in complex with an beta-Phe-AMP analog
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