1aac

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1aac" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aac, resolution 1.31&Aring;" /> '''AMICYANIN OXIDIZED, ...)
Current revision (06:29, 7 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1aac.gif|left|200px]]<br /><applet load="1aac" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1aac, resolution 1.31&Aring;" />
 
-
'''AMICYANIN OXIDIZED, 1.31 ANGSTROMS'''<br />
 
-
==Overview==
+
==AMICYANIN OXIDIZED, 1.31 ANGSTROMS==
-
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.
+
<StructureSection load='1aac' size='340' side='right'caption='[[1aac]], [[Resolution|resolution]] 1.31&Aring;' scene=''>
 +
== 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>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.31&#8491;</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>
 +
</table>
 +
== 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 ==
 +
[[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/aa/1aac_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=1aac ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1AAC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AAC OCA].
+
*[[Amicyanin 3D structures|Amicyanin 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
X-ray structure of the cupredoxin amicyanin, from Paracoccus denitrificans, refined at 1.31 A resolution., Cunane LM, Chen ZW, Durley RC, Mathews FS, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):676-86. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299631 15299631]
+
[[Category: Large Structures]]
[[Category: Paracoccus denitrificans]]
[[Category: Paracoccus denitrificans]]
-
[[Category: Single protein]]
+
[[Category: Chen Z-W]]
-
[[Category: Chen, Z.W.]]
+
[[Category: Cunane LM]]
-
[[Category: Cunane, L.M.]]
+
[[Category: Durley RCE]]
-
[[Category: Durley, R.C.E.]]
+
[[Category: Mathews FS]]
-
[[Category: Mathews, F.S.]]
+
-
[[Category: CU]]
+
-
[[Category: electron transport]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:42:57 2007''
+

Current revision

AMICYANIN OXIDIZED, 1.31 ANGSTROMS

PDB ID 1aac

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools