1r51: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(2 intermediate revisions by the same user not shown)
Line 1: Line 1:


==URATE OXIDASE FROM ASPERGILLUS FLAVUS COMPLEXED WITH ITS INHIBITOR 8-AZAXANTHIN==
==URATE OXIDASE FROM ASPERGILLUS FLAVUS COMPLEXED WITH ITS INHIBITOR 8-AZAXANTHIN==
<StructureSection load='1r51' size='340' side='right' caption='[[1r51]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='1r51' size='340' side='right'caption='[[1r51]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1r51]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1uox 1uox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R51 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R51 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1r51]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1uox 1uox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R51 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AZA:8-AZAXANTHINE'>AZA</scene>, <scene name='pdbligand=CYS:CYSTEINE'>CYS</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]] 1.75&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZA:8-AZAXANTHINE'>AZA</scene>, <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uox|1uox]]</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=1r51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r51 OCA], [https://pdbe.org/1r51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r51 RCSB], [https://www.ebi.ac.uk/pdbsum/1r51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r51 ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Factor_independent_urate_hydroxylase Factor independent urate hydroxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] </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=1r51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r51 OCA], [http://pdbe.org/1r51 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r51 RCSB], [http://www.ebi.ac.uk/pdbsum/1r51 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r51 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/URIC_ASPFL URIC_ASPFL]] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.  
[https://www.uniprot.org/uniprot/URIC_ASPFL URIC_ASPFL] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 31: Line 29:
</div>
</div>
<div class="pdbe-citations 1r51" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1r51" style="background-color:#fffaf0;"></div>
==See Also==
*[[Urate oxidase 3D structures|Urate oxidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
Line 36: Line 37:
</StructureSection>
</StructureSection>
[[Category: Aspergillus flavus]]
[[Category: Aspergillus flavus]]
[[Category: Factor independent urate hydroxylase]]
[[Category: Large Structures]]
[[Category: Prange, T]]
[[Category: Colloc'h N]]
[[Category: Retailleau, P]]
[[Category: Prange T]]
[[Category: H, N Colloc]]
[[Category: Retailleau P]]
[[Category: Dimeric barrel]]
[[Category: Oxidoreductase]]
[[Category: Tunnel-shaped protein]]
[[Category: Uric acid degradation]]

Latest revision as of 09:01, 23 August 2023

URATE OXIDASE FROM ASPERGILLUS FLAVUS COMPLEXED WITH ITS INHIBITOR 8-AZAXANTHINURATE OXIDASE FROM ASPERGILLUS FLAVUS COMPLEXED WITH ITS INHIBITOR 8-AZAXANTHIN

Structural highlights

1r51 is a 1 chain structure with sequence from Aspergillus flavus. This structure supersedes the now removed PDB entry 1uox. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

URIC_ASPFL Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

High-resolution X-ray structures of the complexes of Aspergillus flavus urate oxidase (Uox) with three inhibitors, 8-azaxanthin (AZA), 9-methyl uric acid (MUA) and oxonic acid (OXC), were determined in an orthorhombic space group (I222). In addition, the ligand-free enzyme was also crystallized in a monoclinic form (P2(1)) and its structure determined. Higher accuracy in the three new enzyme-inhibitor complex structures (Uox-AZA, Uox-MUA and Uox-OXC) with respect to the previously determined structure of Uox-AZA (PDB code 1uox) leads to a reversed position of the inhibitor in the active site of the enzyme. The corrected anchoring of the substrate (uric acid) allows an improvement in the understanding of the enzymatic mechanism of urate oxidase.

Complexed and ligand-free high-resolution structures of urate oxidase (Uox) from Aspergillus flavus: a reassignment of the active-site binding mode.,Retailleau P, Colloc'h N, Vivares D, Bonnete F, Castro B, El-Hajji M, Mornon JP, Monard G, Prange T Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):453-62. Epub 2004, Feb 25. PMID:14993669[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Retailleau P, Colloc'h N, Vivares D, Bonnete F, Castro B, El-Hajji M, Mornon JP, Monard G, Prange T. Complexed and ligand-free high-resolution structures of urate oxidase (Uox) from Aspergillus flavus: a reassignment of the active-site binding mode. Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):453-62. Epub 2004, Feb 25. PMID:14993669 doi:http://dx.doi.org/10.1107/S0907444903029718

1r51, resolution 1.75Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA