1uf7: Difference between revisions

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New page: left|200px<br /><applet load="1uf7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uf7, resolution 1.90Å" /> '''Crystal structure of...
 
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[[Image:1uf7.gif|left|200px]]<br /><applet load="1uf7" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1uf7, resolution 1.90&Aring;" />
'''Crystal structure of C171A/V236A Mutant of N-carbamyl-D-amino acid amidohydrolase complexed with N-carbamyl-D-valine'''<br />


==About this Structure==
==Crystal structure of C171A/V236A Mutant of N-carbamyl-D-amino acid amidohydrolase complexed with N-carbamyl-D-valine==
1UF7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_sp. Agrobacterium sp.] with CDV as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UF7 OCA].  
<StructureSection load='1uf7' size='340' side='right'caption='[[1uf7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
[[Category: Agrobacterium sp.]]
== Structural highlights ==
[[Category: N-carbamoyl-D-amino acid hydrolase]]
<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>
[[Category: Single protein]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
[[Category: Aoki, M.]]
<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>
[[Category: Hashimoto, H.]]
<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>
[[Category: Ikenaka, Y.]]
</table>
[[Category: Morikawa, H.]]
== Function ==
[[Category: Nakai, T.]]
[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.
[[Category: Sato, M.]]
== Evolutionary Conservation ==
[[Category: Shimizu, T.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Takahashi, S.]]
Check<jmol>
[[Category: CDV]]
  <jmolCheckbox>
[[Category: d-amino acid]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uf/1uf7_consurf.spt"</scriptWhenChecked>
[[Category: hydrolase]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: n-carbamyl-d-amino acid amidohydrolase]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: n-carbamyl-d-valine]]
  </jmolCheckbox>
 
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1uf7 ConSurf].
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:05:04 2007''
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Agrobacterium sp]]
[[Category: Large Structures]]
[[Category: Aoki M]]
[[Category: Hashimoto H]]
[[Category: Ikenaka Y]]
[[Category: Morikawa H]]
[[Category: Nakai T]]
[[Category: Sato M]]
[[Category: Shimizu T]]
[[Category: Takahashi S]]

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

1uf7 is a 2 chain structure with sequence from Agrobacterium sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1uf7, resolution 1.90Å

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