2hmq: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2hmq.gif|left|200px]]


<!--
==THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION==
The line below this paragraph, containing "STRUCTURE_2hmq", creates the "Structure Box" on the page.
<StructureSection load='2hmq' size='340' side='right'caption='[[2hmq]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2hmq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Themiste_dyscritum Themiste dyscritum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HMQ FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.66&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene></td></tr>
{{STRUCTURE_2hmq| PDB=2hmq  | SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hmq OCA], [https://pdbe.org/2hmq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hmq RCSB], [https://www.ebi.ac.uk/pdbsum/2hmq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hmq ProSAT]</span></td></tr>
 
</table>
'''THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION'''
== Function ==
 
[https://www.uniprot.org/uniprot/HEMT_THEDY HEMT_THEDY] Hemerythrin is a respiratory protein in blood cells of certain marine worms. The oxygen-binding site in each chain contains two iron atoms.
 
== Evolutionary Conservation ==
==Overview==
[[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/hm/2hmq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2hmq ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystallographic refinement of met and azidomet hemerythrin has been carried out at 1.66 A resolution in an attempt to characterize precisely the binuclear iron center in this protein. Restrained least-squares refinement has produced molecular models giving R-values of 18.9% for met (65,683 reflections from 10 A to 1.66 A) and 17.6% for azidomet hemerythrin (68,747 reflections from 10.0 A to 1.66 A). The protein structure in each derivative is very similar to that of myohemerythrin. The mu-oxo bridged iron center differs between the two forms. The complex in met hemerythrin is asymmetric with the bridging oxygen closer to one of the iron atoms while the complex in azidomet hemerythrin is symmetric. After investigations of the effects of correlation in the refinement, we believe this difference between the two complexes is associated with chemical differences and is not a refinement artefact.
The crystallographic refinement of met and azidomet hemerythrin has been carried out at 1.66 A resolution in an attempt to characterize precisely the binuclear iron center in this protein. Restrained least-squares refinement has produced molecular models giving R-values of 18.9% for met (65,683 reflections from 10 A to 1.66 A) and 17.6% for azidomet hemerythrin (68,747 reflections from 10.0 A to 1.66 A). The protein structure in each derivative is very similar to that of myohemerythrin. The mu-oxo bridged iron center differs between the two forms. The complex in met hemerythrin is asymmetric with the bridging oxygen closer to one of the iron atoms while the complex in azidomet hemerythrin is symmetric. After investigations of the effects of correlation in the refinement, we believe this difference between the two complexes is associated with chemical differences and is not a refinement artefact.


==About this Structure==
Structures of met and azidomet hemerythrin at 1.66 A resolution.,Holmes MA, Stenkamp RE J Mol Biol. 1991 Aug 5;220(3):723-37. PMID:1870128<ref>PMID:1870128</ref>
2HMQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Themiste_dyscritum Themiste dyscritum]. This structure supersedes the now removed PDB entries  and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hmn 1hmn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HMQ OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structures of met and azidomet hemerythrin at 1.66 A resolution., Holmes MA, Stenkamp RE, J Mol Biol. 1991 Aug 5;220(3):723-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1870128 1870128]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 2hmq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Themiste dyscritum]]
[[Category: Themiste dyscritum]]
[[Category: Holmes, M A.]]
[[Category: Holmes MA]]
[[Category: Stenkamp, R E.]]
[[Category: Stenkamp RE]]
[[Category: Oxygen transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:28:07 2008''

Latest revision as of 08:12, 13 August 2026

THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION

2hmq, resolution 1.66Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2hmq&oldid=4477158"