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.


2h2w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:54, 20 September 2023) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2h2w.gif|left|200px]]
 
-
{{Structure
+
==Crystal structure of Homoserine O-succinyltransferase (EC 2.3.1.46) (Homoserine O-transsuccinylase) (HTS) (tm0881) from THERMOTOGA MARITIMA at 2.52 A resolution==
-
|PDB= 2h2w |SIZE=350|CAPTION= <scene name='initialview01'>2h2w</scene>, resolution 2.520&Aring;
+
<StructureSection load='2h2w' size='340' side='right'caption='[[2h2w]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[2h2w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H2W FirstGlance]. <br>
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_O-succinyltransferase Homoserine O-succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.46 2.3.1.46] </span>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.52&#8491;</td></tr>
-
|GENE= metA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2w OCA], [https://pdbe.org/2h2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h2w RCSB], [https://www.ebi.ac.uk/pdbsum/2h2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h2w ProSAT], [https://www.topsan.org/Proteins/JCSG/2h2w TOPSAN]</span></td></tr>
-
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd03131 GATase1_HTS]</span>
+
</table>
-
|RELATEDENTRY=
+
== Function ==
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2w OCA], [http://www.ebi.ac.uk/pdbsum/2h2w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h2w RCSB]</span>
+
[https://www.uniprot.org/uniprot/METAA_THEMA METAA_THEMA] Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. Utilizes a ping-pong kinetic mechanism in which the acetyl group of acetyl-CoA is initially transferred to the enzyme to form an acetyl-enzyme intermediate before subsequent transfer to homoserine to form the final product, O-acetylhomoserine. Has weak activity with succinyl-CoA as the acyl donor.<ref>PMID:16708165</ref>
-
}}
+
== Evolutionary Conservation ==
-
 
+
[[Image:Consurf_key_small.gif|200px|right]]
-
'''Crystal structure of Homoserine O-succinyltransferase (EC 2.3.1.46) (Homoserine O-transsuccinylase) (HTS) (tm0881) from THERMOTOGA MARITIMA at 2.52 A resolution'''
+
Check<jmol>
-
 
+
<jmolCheckbox>
-
 
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/2h2w_consurf.spt"</scriptWhenChecked>
-
==About this Structure==
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
2H2W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2W OCA].
+
<text>to colour the structure by Evolutionary Conservation</text>
-
[[Category: Homoserine O-succinyltransferase]]
+
</jmolCheckbox>
-
[[Category: Single protein]]
+
</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=2h2w ConSurf].
 +
<div style="clear:both"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
-
[[Category: JCSG, Joint Center for Structural Genomics.]]
 
-
[[Category: (ec 2 3.1 46)]]
 
-
[[Category: (tm0881)]]
 
-
[[Category: homoserine o-succinyltransferase]]
 
-
[[Category: homoserine o-transsuccinylase]]
 
-
[[Category: ht]]
 
-
[[Category: jcsg]]
 
-
[[Category: joint center for structural genomic]]
 
-
[[Category: protein structure initiative]]
 
-
[[Category: psi]]
 
-
[[Category: structural genomic]]
 
-
[[Category: tm0881]]
 
- 
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:24:42 2008''
 

Current revision

Crystal structure of Homoserine O-succinyltransferase (EC 2.3.1.46) (Homoserine O-transsuccinylase) (HTS) (tm0881) from THERMOTOGA MARITIMA at 2.52 A resolution

PDB ID 2h2w

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/2h2w"
Personal tools