1mcx: Difference between revisions

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


{{STRUCTURE_1mcx|  PDB=1mcx  |  SCENE=  }}
==STRUCTURE OF FULL-LENGTH ANNEXIN A1 IN THE PRESENCE OF CALCIUM==
 
<StructureSection load='1mcx' size='340' side='right'caption='[[1mcx]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
===STRUCTURE OF FULL-LENGTH ANNEXIN A1 IN THE PRESENCE OF CALCIUM===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1mcx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MCX FirstGlance]. <br>
{{ABSTRACT_PUBMED_12595246}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1mcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mcx OCA], [https://pdbe.org/1mcx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mcx RCSB], [https://www.ebi.ac.uk/pdbsum/1mcx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mcx ProSAT]</span></td></tr>
[[1mcx]] is a 1 chain structure of [[Annexin]] with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MCX OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/ANXA1_PIG ANXA1_PIG] Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity.
== 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/mc/1mcx_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=1mcx ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Annexin|Annexin]]
*[[Annexin 3D structures|Annexin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:012595246</ref><references group="xtra"/>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Luecke, H.]]
[[Category: Luecke H]]
[[Category: Rosengarth, A.]]
[[Category: Rosengarth A]]
[[Category: Calcium/phospholipid binding protein]]
[[Category: Metal binding protein]]

Latest revision as of 11:34, 10 April 2024

STRUCTURE OF FULL-LENGTH ANNEXIN A1 IN THE PRESENCE OF CALCIUMSTRUCTURE OF FULL-LENGTH ANNEXIN A1 IN THE PRESENCE OF CALCIUM

Structural highlights

1mcx is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.03Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ANXA1_PIG Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity.

Evolutionary Conservation

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

See Also

1mcx, resolution 2.03Å

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