2fal: Difference between revisions
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<StructureSection load='2fal' size='340' side='right'caption='[[2fal]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='2fal' size='340' side='right'caption='[[2fal]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2fal]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2fal]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aplysia_limacina Aplysia limacina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FAL FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fal OCA], [https://pdbe.org/2fal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fal RCSB], [https://www.ebi.ac.uk/pdbsum/2fal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fal ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fal OCA], [https://pdbe.org/2fal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fal RCSB], [https://www.ebi.ac.uk/pdbsum/2fal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fal ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/GLB_APLLI GLB_APLLI] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aplysia limacina]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ascenzi | [[Category: Ascenzi P]] | ||
[[Category: Bolognesi | [[Category: Bolognesi M]] | ||
[[Category: Brunori | [[Category: Brunori M]] | ||
[[Category: Coda | [[Category: Coda A]] | ||
[[Category: Conti | [[Category: Conti E]] | ||
[[Category: Lionetti | [[Category: Lionetti C]] | ||
[[Category: Mattevi | [[Category: Mattevi A]] | ||
[[Category: Moser | [[Category: Moser C]] | ||
[[Category: Rizzi | [[Category: Rizzi M]] | ||
Revision as of 08:38, 5 June 2024
X-RAY CRYSTAL STRUCTURE OF FERRIC APLYSIA LIMACINA MYOGLOBIN IN DIFFERENT LIGANDED STATESX-RAY CRYSTAL STRUCTURE OF FERRIC APLYSIA LIMACINA MYOGLOBIN IN DIFFERENT LIGANDED STATES
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe X-ray crystal structure of the ligand-free ferric form of Aplysia limacina myoglobin (pH 6.0) has been refined at 1.7 A resolution (R = 15.1%), and its cyanide, thiocyanate and imidazole derivatives studied by difference Fourier techniques at atomic resolution. The crystallographic R-factors of the three different derivatives reported are 16.1%, 16.1% and 15.6% at 1.8 A, 2.0 A and 2.0 A resolution, respectively. The present results have been analyzed in parallel with previous crystallographic studies on the molecular structures of the fluoride and azide derivatives of ferric Aplysia limacina myoglobin. Ligand binding to the distal site of the heme pocket results in different networks of hydrogen bonds involving to various degrees the bound ligand, residue Arg(66)E10, the heme propionate III, ordered water molecules and/or protein backbone atoms from the CD region. In particular, Arg(66)E10 stabilizes the bound ligand and compensates for the absence of the hydrogen bond donor residue HisE7, commonly present in oxygen-carrying globins. X-ray crystal structure of ferric Aplysia limacina myoglobin in different liganded states.,Conti E, Moser C, Rizzi M, Mattevi A, Lionetti C, Coda A, Ascenzi P, Brunori M, Bolognesi M J Mol Biol. 1993 Oct 5;233(3):498-508. PMID:8411158[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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