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.


4uqv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:33, 10 January 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==methanococcus jannaschii serine hydroxymethyl-transferase in complex with PLP==
==methanococcus jannaschii serine hydroxymethyl-transferase in complex with PLP==
-
<StructureSection load='4uqv' size='340' side='right' caption='[[4uqv]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+
<StructureSection load='4uqv' size='340' side='right'caption='[[4uqv]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4uqv]] is a 12 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bhe 4bhe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UQV FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4uqv]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bhe 4bhe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UQV FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uqv RCSB], [http://www.ebi.ac.uk/pdbsum/4uqv PDBsum]</span></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></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=4uqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqv OCA], [https://pdbe.org/4uqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uqv RCSB], [https://www.ebi.ac.uk/pdbsum/4uqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uqv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA]] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref>
+
[https://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 16: Line 18:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
<div class="pdbe-citations 4uqv" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Angelucci, F]]
+
[[Category: Large Structures]]
-
[[Category: Ilari, A]]
+
[[Category: Methanocaldococcus jannaschii]]
-
[[Category: Saccoccia, F]]
+
[[Category: Angelucci F]]
-
[[Category: Serine hydroxymethyl-transferase]]
+
[[Category: Ilari A]]
-
[[Category: Transferase]]
+
[[Category: Saccoccia F]]

Current revision

methanococcus jannaschii serine hydroxymethyl-transferase in complex with PLP

PDB ID 4uqv

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools