3hq2: Difference between revisions

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[[Image:3hq2.png|left|200px]]


{{STRUCTURE_3hq2|  PDB=3hq2  |  SCENE= }}
==BsuCP Crystal Structure==
 
<StructureSection load='3hq2' size='340' side='right'caption='[[3hq2]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
===BsuCP Crystal Structure===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3hq2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HQ2 FirstGlance]. <br>
{{ABSTRACT_PUBMED_19544567}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <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=3hq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hq2 OCA], [https://pdbe.org/3hq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hq2 RCSB], [https://www.ebi.ac.uk/pdbsum/3hq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hq2 ProSAT]</span></td></tr>
[[3hq2]] is a 2 chain structure of [[Carboxypeptidase]] with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HQ2 OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/CBP1_BACSU CBP1_BACSU] Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues. Has lower activity with substrates ending with His or Trp.<ref>PMID:19544567</ref>
== 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/hq/3hq2_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=3hq2 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Carboxypeptidase|Carboxypeptidase]]
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:019544567</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Chan, M K.]]
[[Category: Large Structures]]
[[Category: Chan, S I.]]
[[Category: Chan MK]]
[[Category: Chen, R P.Y.]]
[[Category: Chan SI]]
[[Category: He, H T.F.]]
[[Category: Chen RP-Y]]
[[Category: Isaza, C E.]]
[[Category: He HT-F]]
[[Category: Lee, M M.]]
[[Category: Isaza CE]]
[[Category: Liang, G F.C.]]
[[Category: Lee MM]]
[[Category: White, J D.]]
[[Category: Liang GF-C]]
[[Category: Hydrolase]]
[[Category: White JD]]
[[Category: Metal-binding]]
[[Category: Metalloprotease]]
[[Category: Protease]]

Latest revision as of 13:01, 21 February 2024

BsuCP Crystal StructureBsuCP Crystal Structure

Structural highlights

3hq2 is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CBP1_BACSU Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues. Has lower activity with substrates ending with His or Trp.[1]

Evolutionary Conservation

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

See Also

References

  1. ↑ Lee MM, Isaza CE, White JD, Chen RP, Liang GF, He HT, Chan SI, Chan MK. Insight into the substrate length restriction of M32 carboxypeptidases: Characterization of two distinct subfamilies. Proteins. 2009 May 11;77(3):647-657. PMID:19544567 doi:10.1002/prot.22478

3hq2, resolution 2.90Å

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OCA
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