1uf7: Difference between revisions
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<StructureSection load='1uf7' size='340' side='right'caption='[[1uf7]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1uf7' size='340' side='right'caption='[[1uf7]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1uf7]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1uf7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_sp. Agrobacterium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UF7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDV:3-METHYL-2-UREIDO-BUTYRIC+ACID'>CDV</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uf7 OCA], [https://pdbe.org/1uf7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uf7 RCSB], [https://www.ebi.ac.uk/pdbsum/1uf7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uf7 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/DCAS_AGRSK DCAS_AGRSK] The enzyme catalyzes the hydrolysis of N-carbamoyl-D-amino acids to the corresponding which are useful intermediates in the preparation of beta-lactam antibiotics. Industrial production of beta-lactam antibiotics is now being developed using this enzyme. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Agrobacterium sp]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Aoki M]] | |||
[[Category: Aoki | [[Category: Hashimoto H]] | ||
[[Category: Hashimoto | [[Category: Ikenaka Y]] | ||
[[Category: Ikenaka | [[Category: Morikawa H]] | ||
[[Category: Morikawa | [[Category: Nakai T]] | ||
[[Category: Nakai | [[Category: Sato M]] | ||
[[Category: Sato | [[Category: Shimizu T]] | ||
[[Category: Shimizu | [[Category: Takahashi S]] | ||
[[Category: Takahashi | |||
Latest revision as of 02:52, 28 December 2023
Crystal structure of C171A/V236A Mutant of N-carbamyl-D-amino acid amidohydrolase complexed with N-carbamyl-D-valineCrystal structure of C171A/V236A Mutant of N-carbamyl-D-amino acid amidohydrolase complexed with N-carbamyl-D-valine
Structural highlights
FunctionDCAS_AGRSK The enzyme catalyzes the hydrolysis of N-carbamoyl-D-amino acids to the corresponding which are useful intermediates in the preparation of beta-lactam antibiotics. Industrial production of beta-lactam antibiotics is now being developed using this enzyme. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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