1erz: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==CRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES== | ==CRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES== | ||
<StructureSection load='1erz' size='340' side='right'caption='[[1erz]]' scene=''> | <StructureSection load='1erz' size='340' side='right'caption='[[1erz]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ERZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ERZ FirstGlance]. <br> | <table><tr><td colspan='2'>[[1erz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_sp._KNK712 Agrobacterium sp. KNK712]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ERZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ERZ FirstGlance]. <br> | ||
</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=1erz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1erz OCA], [https://pdbe.org/1erz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1erz RCSB], [https://www.ebi.ac.uk/pdbsum/1erz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1erz ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</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=1erz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1erz OCA], [https://pdbe.org/1erz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1erz RCSB], [https://www.ebi.ac.uk/pdbsum/1erz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1erz ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== 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]] | ||
| Line 18: | Line 21: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Agrobacterium sp. KNK712]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hasegawa T]] | [[Category: Hasegawa T]] | ||
Latest revision as of 07:06, 7 February 2024
CRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES
| ||||||||||||
