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.


4xz2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:51, 10 January 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Human platelet phosphofructokinase in an R-state in complex with ADP and F6P, crystal form I==
==Human platelet phosphofructokinase in an R-state in complex with ADP and F6P, crystal form I==
-
<StructureSection load='4xz2' size='340' side='right' caption='[[4xz2]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
+
<StructureSection load='4xz2' size='340' side='right'caption='[[4xz2]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4xz2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XZ2 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4xz2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XZ2 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.67&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wlo|4wlo]], [[4u1r|4u1r]], [[4rh3|4rh3]], [[4omt|4omt]], [[3opy|3opy]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/6-phosphofructokinase 6-phosphofructokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.11 2.7.1.11] </span></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=4xz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xz2 OCA], [https://pdbe.org/4xz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xz2 RCSB], [https://www.ebi.ac.uk/pdbsum/4xz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xz2 ProSAT]</span></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=4xz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xz2 OCA], [http://pdbe.org/4xz2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xz2 RCSB], [http://www.ebi.ac.uk/pdbsum/4xz2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xz2 ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/PFKAP_HUMAN PFKAP_HUMAN]] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
+
[https://www.uniprot.org/uniprot/PFKAP_HUMAN PFKAP_HUMAN] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 20: Line 19:
</div>
</div>
<div class="pdbe-citations 4xz2" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4xz2" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Phosphofructokinase 3D structures|Phosphofructokinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: 6-phosphofructokinase]]
+
[[Category: Homo sapiens]]
-
[[Category: Kloos, M]]
+
[[Category: Large Structures]]
-
[[Category: Strater, N]]
+
[[Category: Kloos M]]
-
[[Category: Fructose 6-phosphate]]
+
[[Category: Strater N]]
-
[[Category: Human platelet phosphofructokinase]]
+
-
[[Category: Main regulator of glycolysis]]
+
-
[[Category: Transferase]]
+

Current revision

Human platelet phosphofructokinase in an R-state in complex with ADP and F6P, crystal form I

PDB ID 4xz2

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools