1aac
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1aac]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AAC FirstGlance]. <br> | <table><tr><td colspan='2'>[[1aac]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AAC FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.31Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=1aac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aac OCA], [https://pdbe.org/1aac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aac RCSB], [https://www.ebi.ac.uk/pdbsum/1aac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aac 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=1aac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aac OCA], [https://pdbe.org/1aac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aac RCSB], [https://www.ebi.ac.uk/pdbsum/1aac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aac ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/AMCY_PARDE AMCY_PARDE] Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1aac ConSurf]. | </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=1aac ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | High-resolution X-ray diffraction data to d(min) = 1.31 A were collected on a Xuong-Hamlin area detector from crystals of the blue-copper protein amicyanin, isolated from P. denitrificans. With coordinates from the earlier 2.0 A structure determination as a starting point, simulated annealing and restrained positional and temperature factor refinements using the program X-PLOR resulted in a final R factor of 15.5%, based on 21 131 unique reflections in the range 8.0-1.3 A. Comparison of the 1.31 A structure with that at 2.0 A shows the same basic features. However, the high-resolution electron-density maps clearly reveal additional solvent molecules and significant discrete disorder in protein side chains and within the solvent structure. As a consequence of modelling side-chain disorder, several new hydrogen-bonding interactions were identified. | ||
| - | + | ==See Also== | |
| - | + | *[[Amicyanin 3D structures|Amicyanin 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Paracoccus denitrificans]] | [[Category: Paracoccus denitrificans]] | ||
| - | [[Category: Chen | + | [[Category: Chen Z-W]] |
| - | [[Category: Cunane | + | [[Category: Cunane LM]] |
| - | [[Category: Durley | + | [[Category: Durley RCE]] |
| - | [[Category: Mathews | + | [[Category: Mathews FS]] |
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Current revision
AMICYANIN OXIDIZED, 1.31 ANGSTROMS
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