We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

5uc9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:25, 4 October 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Crystal structure of human Heme Oxygenase-2 in complex with Myristate==
==Crystal structure of human Heme Oxygenase-2 in complex with Myristate==
-
<StructureSection load='5uc9' size='340' side='right' caption='[[5uc9]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+
<StructureSection load='5uc9' size='340' side='right'caption='[[5uc9]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5uc9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UC9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UC9 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5uc9]] 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=5UC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UC9 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</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]] 1.903&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uc8|5uc8]], [[5uca|5uca]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase_(biliverdin-producing) Heme oxygenase (biliverdin-producing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.18 1.14.14.18] </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=5uc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uc9 OCA], [https://pdbe.org/5uc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uc9 RCSB], [https://www.ebi.ac.uk/pdbsum/5uc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uc9 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=5uc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uc9 OCA], [http://pdbe.org/5uc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uc9 RCSB], [http://www.ebi.ac.uk/pdbsum/5uc9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uc9 ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/HMOX2_HUMAN HMOX2_HUMAN]] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
+
[https://www.uniprot.org/uniprot/HMOX2_HUMAN HMOX2_HUMAN] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
<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 5uc9" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5uc9" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Luo, S]]
+
[[Category: Homo sapiens]]
-
[[Category: Tong, L]]
+
[[Category: Large Structures]]
-
[[Category: Heme oxygenase]]
+
[[Category: Luo S]]
-
[[Category: Myristic acid]]
+
[[Category: Tong L]]
-
[[Category: Oxidoreductase]]
+

Current revision

Crystal structure of human Heme Oxygenase-2 in complex with Myristate

PDB ID 5uc9

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/5uc9"
Personal tools