2f5v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:36, 9 October 2024) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Reaction geometry and thermostability mutant of pyranose 2-oxidase from the white-rot fungus Peniophora sp.==
==Reaction geometry and thermostability mutant of pyranose 2-oxidase from the white-rot fungus Peniophora sp.==
-
<StructureSection load='2f5v' size='340' side='right' caption='[[2f5v]], [[Resolution|resolution]] 1.41&Aring;' scene=''>
+
<StructureSection load='2f5v' size='340' side='right'caption='[[2f5v]], [[Resolution|resolution]] 1.41&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2f5v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Peniophora_sp._sg Peniophora sp. sg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F5V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F5V FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2f5v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Peniophora_sp._SG Peniophora sp. SG]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F5V FirstGlance]. <br>
-
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=KBG:2-KETO-BETA-D-GLUCOSE'>KBG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene><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]] 1.41&#8491;</td></tr>
-
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tzl|1tzl]], [[2f6c|2f6c]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=KBG:2-KETO-BETA-D-GLUCOSE'>KBG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
-
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">p2ox, poxSG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=204723 Peniophora sp. SG])</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=2f5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f5v OCA], [https://pdbe.org/2f5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f5v RCSB], [https://www.ebi.ac.uk/pdbsum/2f5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f5v ProSAT]</span></td></tr>
-
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyranose_oxidase Pyranose oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.10 1.1.3.10] </span></td></tr>
+
</table>
-
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f5v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2f5v RCSB], [http://www.ebi.ac.uk/pdbsum/2f5v PDBsum]</span></td></tr>
+
== Function ==
-
<table>
+
[https://www.uniprot.org/uniprot/P2OX_PENSG P2OX_PENSG] Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O(2) to H(2)O(2). Plays an important role in lignin degradation of wood rot fungi by supplying the essential cosubstrate H(2)O(2) for the ligninolytic peroxidases, lignin peroxidase and manganese-dependent peroxidase (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
-
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f5/2f5v_consurf.spt"</scriptWhenChecked>
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f5/2f5v_consurf.spt"</scriptWhenChecked>
-
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
-
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2f5v ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
Line 27: Line 28:
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 2f5v" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Pyranose oxidase|Pyranose oxidase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Peniophora sp. sg]]
+
[[Category: Large Structures]]
-
[[Category: Pyranose oxidase]]
+
[[Category: Peniophora sp. SG]]
-
[[Category: Bannwarth, M.]]
+
[[Category: Bannwarth M]]
-
[[Category: Bastian, S.]]
+
[[Category: Bastian S]]
-
[[Category: Giffhorn, F.]]
+
[[Category: Giffhorn F]]
-
[[Category: Heckmann-Pohl, D.]]
+
[[Category: Heckmann-Pohl D]]
-
[[Category: Schulz, G E.]]
+
[[Category: Schulz GE]]
-
[[Category: D2]]
+
-
[[Category: Flavoprotein]]
+
-
[[Category: Glutathion-reductase related fold]]
+
-
[[Category: Gmc oxidoreductase]]
+
-
[[Category: Oxidoreductase]]
+
-
[[Category: Phbh-fold]]
+
-
[[Category: Rossmann-fold]]
+
-
[[Category: Tetramer]]
+

Current revision

Reaction geometry and thermostability mutant of pyranose 2-oxidase from the white-rot fungus Peniophora sp.

PDB ID 2f5v

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools