1dpb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:57, 7 February 2024) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1dpb.png|left|200px]]
 
-
<!--
+
==CRYSTALLOGRAPHIC AND ENZYMATIC INVESTIGATIONS ON THE ROLE OF SER558, HIS610 AND ASN614 IN THE CATALYTIC MECHANISM OF AZOTOBACTER VINELANDII DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P)==
-
The line below this paragraph, containing "STRUCTURE_1dpb", creates the "Structure Box" on the page.
+
<StructureSection load='1dpb' size='340' side='right'caption='[[1dpb]], [[Resolution|resolution]] 2.50&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'>[[1dpb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DPB 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]] 2.5&#8491;</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=1dpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpb OCA], [https://pdbe.org/1dpb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dpb RCSB], [https://www.ebi.ac.uk/pdbsum/1dpb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dpb ProSAT]</span></td></tr>
-
{{STRUCTURE_1dpb| PDB=1dpb | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ODP2_AZOVI ODP2_AZOVI] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
 +
== 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/dp/1dpb_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=1dpb ConSurf].
 +
<div style="clear:both"></div>
-
===CRYSTALLOGRAPHIC AND ENZYMATIC INVESTIGATIONS ON THE ROLE OF SER558, HIS610 AND ASN614 IN THE CATALYTIC MECHANISM OF AZOTOBACTER VINELANDII DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P)===
+
==See Also==
-
 
+
*[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]]
-
 
+
__TOC__
-
<!--
+
</StructureSection>
-
The line below this paragraph, {{ABSTRACT_PUBMED_7703242}}, adds the Publication Abstract to the page
+
-
(as it appears on PubMed at http://www.pubmed.gov), where 7703242 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_7703242}}
+
-
 
+
-
==About this Structure==
+
-
1DPB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DPB OCA].
+
-
 
+
-
==Reference==
+
-
Crystallographic and enzymatic investigations on the role of Ser558, His610, and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p)., Hendle J, Mattevi A, Westphal AH, Spee J, de Kok A, Teplyakov A, Hol WG, Biochemistry. 1995 Apr 4;34(13):4287-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7703242 7703242]
+
[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
-
[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Hendle J]]
-
[[Category: Hendle, J.]]
+
[[Category: Hol WGJ]]
-
[[Category: Hol, W G.J.]]
+
-
[[Category: Dihydrolipoamide acetyltransferase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:24:49 2008''
+

Current revision

CRYSTALLOGRAPHIC AND ENZYMATIC INVESTIGATIONS ON THE ROLE OF SER558, HIS610 AND ASN614 IN THE CATALYTIC MECHANISM OF AZOTOBACTER VINELANDII DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P)

PDB ID 1dpb

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools