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[[Image:1nba.gif|left|200px]]


{{Structure
==CRYSTAL STRUCTURE ANALYSIS, REFINEMENT AND ENZYMATIC REACTION MECHANISM OF N-CARBAMOYLSARCOSINE AMIDOHYDROLASE FROM ARTHROBACTER SP. AT 2.0 ANGSTROMS RESOLUTION==
|PDB= 1nba |SIZE=350|CAPTION= <scene name='initialview01'>1nba</scene>, resolution 2.0&Aring;
<StructureSection load='1nba' size='340' side='right'caption='[[1nba]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[1nba]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NBA FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/N-carbamoylsarcosine_amidase N-carbamoylsarcosine amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.59 3.5.1.59] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nba OCA], [https://pdbe.org/1nba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nba RCSB], [https://www.ebi.ac.uk/pdbsum/1nba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nba ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nba OCA], [http://www.ebi.ac.uk/pdbsum/1nba PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nba RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/CSH_ARTSP CSH_ARTSP]
 
== Evolutionary Conservation ==
'''CRYSTAL STRUCTURE ANALYSIS, REFINEMENT AND ENZYMATIC REACTION MECHANISM OF N-CARBAMOYLSARCOSINE AMIDOHYDROLASE FROM ARTHROBACTER SP. AT 2.0 ANGSTROMS RESOLUTION'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nb/1nba_consurf.spt"</scriptWhenChecked>
N-carbamoylsarcosine amidohydrolase from Arthrobacter sp., a tetramer of polypeptides with 264 amino acid residues each, has been crystallized and its structure solved and refined at 2.0 A resolution, to a crystallographic R-factor of 18.6%. The crystals employed in the analysis contain one tetramer of 116,000 M(r) in the asymmetric unit. The structure determination proceeded by multiple isomorphous replacement, followed by solvent-flattening and density averaging about the local diads within the tetramer. In the final refined model, the root-mean-square deviation from ideality is 0.01 A for bond distances and 2.7 degrees for bond angles. The asymmetric unit consists of 7853 protein atoms, 431 water molecules and four sulfate ions bound into the putative active site clefts in each subunit. One subunit contains a central six-stranded parallel beta-pleated sheet packed by helices on both sides. On one side, two helices face the solvent, while two of the helices on the other side are buried in the tight intersubunit contacts. The catalytic center of the enzyme, tentatively identified by inhibitor binding, is located at the interface between two subunits and involves residues from both. It is suggested that the nucleophilic group involved in hydrolysis of the substrate is the thiol group of Cys117 and a nucleophilic addition-elimination mechanism is proposed.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1NBA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NBA OCA].  
</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=1nba ConSurf].
 
<div style="clear:both"></div>
==Reference==
__TOC__
Crystal structure analysis, refinement and enzymatic reaction mechanism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0 A resolution., Romao MJ, Turk D, Gomis-Ruth FX, Huber R, Schumacher G, Mollering H, Russmann L, J Mol Biol. 1992 Aug 20;226(4):1111-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1381445 1381445]
</StructureSection>
[[Category: Arthrobacter sp.]]
[[Category: Arthrobacter sp]]
[[Category: N-carbamoylsarcosine amidase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Gomis-Ruth F-Z]]
[[Category: Gomis-Ruth, F Z.]]
[[Category: Huber R]]
[[Category: Huber, R.]]
[[Category: Mollering H]]
[[Category: Mollering, H.]]
[[Category: Romao MJ]]
[[Category: Romao, M J.]]
[[Category: Russmann L]]
[[Category: Russmann, L.]]
[[Category: Schumacher G]]
[[Category: Schumacher, G.]]
[[Category: Turk D]]
[[Category: Turk, D.]]
[[Category: hydrolase(in linear amides)]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:27:58 2008''

Latest revision as of 07:54, 14 February 2024

CRYSTAL STRUCTURE ANALYSIS, REFINEMENT AND ENZYMATIC REACTION MECHANISM OF N-CARBAMOYLSARCOSINE AMIDOHYDROLASE FROM ARTHROBACTER SP. AT 2.0 ANGSTROMS RESOLUTION

1nba, resolution 2.00Å

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