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1uf8
From Proteopedia
(Difference between revisions)
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<StructureSection load='1uf8' size='340' side='right'caption='[[1uf8]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1uf8' size='340' side='right'caption='[[1uf8]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1uf8]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1uf8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrsp Agrsp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UF8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ING:D-[(AMINO)CARBONYL]PHENYLALANINE'>ING</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ING:D-[(AMINO)CARBONYL]PHENYLALANINE'>ING</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1erz|1erz]], [[1uf4|1uf4]], [[1uf5|1uf5]], [[1uf7|1uf7]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1erz|1erz]], [[1uf4|1uf4]], [[1uf5|1uf5]], [[1uf7|1uf7]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/N-carbamoyl-D-amino-acid_hydrolase N-carbamoyl-D-amino-acid hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.77 3.5.1.77] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uf8 OCA], [https://pdbe.org/1uf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uf8 RCSB], [https://www.ebi.ac.uk/pdbsum/1uf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uf8 ProSAT]</span></td></tr> |
</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]] | ||
Revision as of 06:09, 6 October 2021
Crystal structure of C171A/V236A Mutant of N-carbamyl-D-amino acid amidohydrolase complexed with N-carbamyl-D-Phenylalanine
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