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


{{STRUCTURE_1ain|  PDB=1ain  |  SCENE=  }}
==CRYSTAL STRUCTURE OF HUMAN ANNEXIN I AT 2.5 ANGSTROMS RESOLUTION==
 
<StructureSection load='1ain' size='340' side='right'caption='[[1ain]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
===CRYSTAL STRUCTURE OF HUMAN ANNEXIN I AT 2.5 ANGSTROMS RESOLUTION===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1ain]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AIN FirstGlance]. <br>
{{ABSTRACT_PUBMED_8453382}}
</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=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=1ain FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ain OCA], [https://pdbe.org/1ain PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ain RCSB], [https://www.ebi.ac.uk/pdbsum/1ain PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ain ProSAT]</span></td></tr>
[[1ain]] is a 1 chain structure of [[Annexin]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AIN OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/ANXA1_HUMAN ANXA1_HUMAN] 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/ai/1ain_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=1ain 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:008453382</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Kim, S H.]]
[[Category: Large Structures]]
[[Category: Calcium-phospholipid binding complex]]
[[Category: Kim S-H]]
[[Category: Calcium/phospholipid binding]]

Latest revision as of 09:30, 7 February 2024

CRYSTAL STRUCTURE OF HUMAN ANNEXIN I AT 2.5 ANGSTROMS RESOLUTIONCRYSTAL STRUCTURE OF HUMAN ANNEXIN I AT 2.5 ANGSTROMS RESOLUTION

Structural highlights

1ain is a 1 chain structure with sequence from Homo sapiens. 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

ANXA1_HUMAN 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

1ain, resolution 2.50Å

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