1rad

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1rad" [edit=sysop:move=sysop])
Current revision (08:21, 14 February 2024) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1rad.png|left|200px]]
 
-
{{STRUCTURE_1rad| PDB=1rad | SCENE= }}
+
==CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY==
 +
<StructureSection load='1rad' size='340' side='right'caption='[[1rad]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1rad]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RAD 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]] 2.5&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1rad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rad OCA], [https://pdbe.org/1rad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rad RCSB], [https://www.ebi.ac.uk/pdbsum/1rad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rad ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PYRB_ECOLI PYRB_ECOLI]
 +
== 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/ra/1rad_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=1rad ConSurf].
 +
<div style="clear:both"></div>
-
===CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY===
+
==See Also==
-
 
+
*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]]
-
{{ABSTRACT_PUBMED_8441751}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Escherichia coli K-12]]
-
[[1rad]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RAD OCA].
+
[[Category: Large Structures]]
-
 
+
[[Category: Gouaux JE]]
-
==Reference==
+
[[Category: Kosman RP]]
-
<ref group="xtra">PMID:008441751</ref><references group="xtra"/>
+
[[Category: Lipscomb WN]]
-
[[Category: Aspartate carbamoyltransferase]]
+
-
[[Category: Escherichia coli]]
+
-
[[Category: Gouaux, J E.]]
+
-
[[Category: Kosman, R P.]]
+
-
[[Category: Lipscomb, W N.]]
+
-
[[Category: Transferase]]
+

Current revision

CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY

PDB ID 1rad

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools