2rgz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:57, 30 August 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='2rgz' size='340' side='right'caption='[[2rgz]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
<StructureSection load='2rgz' size='340' side='right'caption='[[2rgz]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2rgz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RGZ FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2rgz]] is a 2 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=2RGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RGZ FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 2.61&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qpp|2qpp]], [[2q32|2q32]]</div></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HMOX2, HO2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=2rgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rgz OCA], [https://pdbe.org/2rgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rgz RCSB], [https://www.ebi.ac.uk/pdbsum/2rgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rgz ProSAT]</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=2rgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rgz OCA], [https://pdbe.org/2rgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rgz RCSB], [https://www.ebi.ac.uk/pdbsum/2rgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rgz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[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.
+
[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 38: Line 36:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Heme oxygenase]]
+
[[Category: Homo sapiens]]
-
[[Category: Human]]
+
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Bianchetti, C M]]
+
[[Category: Bianchetti CM]]
-
[[Category: Bingman, C A]]
+
[[Category: Bingman CA]]
-
[[Category: Bitto, E]]
+
[[Category: Bitto E]]
-
[[Category: Structural genomic]]
+
[[Category: Phillips Jr GN]]
-
[[Category: Phillips, G N]]
+
[[Category: Wesenberg GE]]
-
[[Category: Wesenberg, G E]]
+
-
[[Category: Cesg]]
+
-
[[Category: Endoplasmic reticulum]]
+
-
[[Category: Ensemble refinement]]
+
-
[[Category: Ho-2]]
+
-
[[Category: Iron]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: Microsome]]
+
-
[[Category: Oxidoreductase]]
+
-
[[Category: PSI, Protein structure initiative]]
+
-
[[Category: Refinement methodology development]]
+

Current revision

Ensemble refinement of the protein crystal structure of human heme oxygenase-2 C127A (HO-2) with bound heme

PDB ID 2rgz

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/2rgz"
Personal tools