4n0w: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
m Protected "4n0w" [edit=sysop:move=sysop]
OCA (talk | contribs)
No edit summary
 
(5 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 4n0w is ON HOLD
==X-ray crystal structure of a serine hydroxymethyltransferase from Burkholderia cenocepacia with covalently attached pyridoxal phosphate==
<StructureSection load='4n0w' size='340' side='right'caption='[[4n0w]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4n0w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cenocepacia_J2315 Burkholderia cenocepacia J2315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N0W 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]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4n0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0w OCA], [https://pdbe.org/4n0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n0w RCSB], [https://www.ebi.ac.uk/pdbsum/4n0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n0w ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B4ECY9_BURCJ B4ECY9_BURCJ] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (By similarity).[HAMAP-Rule:MF_00051]


Authors: Seattle Structural Genomics Center for Infectious Disease (SSGCID)
==See Also==
 
*[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]]
Description: X-ray crystal structure of a serine hydroxymethyltransferase from Burkholderia cenocepacia with covalently attached pyridoxal phosphate
__TOC__
</StructureSection>
[[Category: Burkholderia cenocepacia J2315]]
[[Category: Large Structures]]

Latest revision as of 16:45, 20 September 2023

X-ray crystal structure of a serine hydroxymethyltransferase from Burkholderia cenocepacia with covalently attached pyridoxal phosphate

4n0w, resolution 1.65Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA