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2ggk
From Proteopedia
(Difference between revisions)
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<StructureSection load='2ggk' size='340' side='right' caption='[[2ggk]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2ggk' size='340' side='right' caption='[[2ggk]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ggk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2ggk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_radiobacter"_(beijerinck_and_van_delden_1902)_bergey_et_al._1934 "achromobacter radiobacter" (beijerinck and van delden 1902) bergey et al. 1934]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2fkv 2fkv] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2ba5 2ba5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GGK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GGK FirstGlance]. <br> |
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fo6|1fo6]], [[2ggl|2ggl]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fo6|1fo6]], [[2ggl|2ggl]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-carbamoyl-D-amino-acid_hydrolase N-carbamoyl-D-amino-acid hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.77 3.5.1.77] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-carbamoyl-D-amino-acid_hydrolase N-carbamoyl-D-amino-acid hydrolase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ggk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ggk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ggk RCSB], [http://www.ebi.ac.uk/pdbsum/2ggk PDBsum]</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=2ggk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ggk OCA], [http://pdbe.org/2ggk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ggk RCSB], [http://www.ebi.ac.uk/pdbsum/2ggk PDBsum]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://www.uniprot.org/uniprot/DCAS_RHIRD DCAS_RHIRD]] 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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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 2ggk" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Agrobacterium tumefaciens]] | ||
[[Category: N-carbamoyl-D-amino-acid hydrolase]] | [[Category: N-carbamoyl-D-amino-acid hydrolase]] | ||
[[Category: Chiu, W C]] | [[Category: Chiu, W C]] | ||
Revision as of 21:26, 9 September 2015
The mutant A302C of Agrobacterium radiobacter N-carbamoyl-D-amino-acid amidohydrolase
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