1cg2: Difference between revisions

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[[Image:1cg2.png|left|200px]]


{{STRUCTURE_1cg2|  PDB=1cg2  |  SCENE= }}
==CARBOXYPEPTIDASE G2==
 
<StructureSection load='1cg2' size='340' side='right'caption='[[1cg2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
===CARBOXYPEPTIDASE G2===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1cg2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._RS-16 Pseudomonas sp. RS-16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CG2 FirstGlance]. <br>
{{ABSTRACT_PUBMED_9083113}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cg2 OCA], [https://pdbe.org/1cg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cg2 RCSB], [https://www.ebi.ac.uk/pdbsum/1cg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cg2 ProSAT]</span></td></tr>
[[1cg2]] is a 4 chain structure of [[Carboxypeptidase]] with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CG2 OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/CBPG_PSES6 CBPG_PSES6] Catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and L-glutamate. This enzyme has a broad specificity.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cg/1cg2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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=1cg2 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Carboxypeptidase|Carboxypeptidase]]
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:009083113</ref><ref group="xtra">PMID:010595564</ref><ref group="xtra">PMID:014579367</ref><references group="xtra"/>
[[Category: Large Structures]]
[[Category: Glutamate carboxypeptidase]]
[[Category: Pseudomonas sp. RS-16]]
[[Category: Pseudomonas sp.]]
[[Category: Blow DM]]
[[Category: Blow, D M.]]
[[Category: Brick P]]
[[Category: Brick, P.]]
[[Category: Melton RG]]
[[Category: Melton, R G.]]
[[Category: Pauptit RA]]
[[Category: Pauptit, R A.]]
[[Category: Rowsell S]]
[[Category: Rowsell, S.]]
[[Category: Tucker AD]]
[[Category: Tucker, A D.]]
[[Category: Hydrolase]]
[[Category: Metallocarboxypeptidase]]

Latest revision as of 10:24, 14 February 2024

CARBOXYPEPTIDASE G2CARBOXYPEPTIDASE G2

Structural highlights

1cg2 is a 4 chain structure with sequence from Pseudomonas sp. RS-16. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CBPG_PSES6 Catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and L-glutamate. This enzyme has a broad specificity.

Evolutionary Conservation

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

See Also

1cg2, resolution 2.50Å

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