This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1aac

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:29, 7 February 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1aac.gif|left|200px]]
 
-
<!--
+
==AMICYANIN OXIDIZED, 1.31 ANGSTROMS==
-
The line below this paragraph, containing "STRUCTURE_1aac", creates the "Structure Box" on the page.
+
<StructureSection load='1aac' size='340' side='right'caption='[[1aac]], [[Resolution|resolution]] 1.31&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'>[[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>
-
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]] 1.31&#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>
-
{{STRUCTURE_1aac| PDB=1aac | SCENE= }}
+
<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>
-
'''AMICYANIN OXIDIZED, 1.31 ANGSTROMS'''
+
==See Also==
-
 
+
*[[Amicyanin 3D structures|Amicyanin 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
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.
+
[[Category: Large Structures]]
-
 
+
-
==About this Structure==
+
-
1AAC is a [[Single protein]] structure of sequence from [http://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].
+
-
 
+
-
==Reference==
+
-
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://www.ncbi.nlm.nih.gov/pubmed/15299631 15299631]
+
[[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: Electron transport]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:02:41 2008''
+

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

Retrieved from "http://52.214.119.220/wiki/index.php/1aac"
Personal tools