1erz
From Proteopedia
(Difference between revisions)
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==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]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Agrobacterium sp. KNK712]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hasegawa T]] | [[Category: Hasegawa T]] | ||
Current revision
CRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES
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Categories: Agrobacterium sp. KNK712 | Large Structures | Hasegawa T | Ikenaka Y | Kumasaka T | Nakai T | Nanba H | Sato M | Takahashi S | Tsukihara T | Ueki T | Yamamoto M | Yamashita E
