4hsl: Difference between revisions

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==2.00 angstrom x-ray crystal structure of substrate-bound E110A 3-hydroxyanthranilate-3,4-dioxygenase from Cupriavidus metallidurans==
==2.00 angstrom x-ray crystal structure of substrate-bound E110A 3-hydroxyanthranilate-3,4-dioxygenase from Cupriavidus metallidurans==
<StructureSection load='4hsl' size='340' side='right' caption='[[4hsl]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4hsl' size='340' side='right' caption='[[4hsl]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cupriavidus metallidurans, nbaC, Rmet_5193 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266264 Cupriavidus metallidurans CH34])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cupriavidus metallidurans, nbaC, Rmet_5193 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266264 Cupriavidus metallidurans CH34])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxyanthranilate_3,4-dioxygenase 3-hydroxyanthranilate 3,4-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.6 1.13.11.6] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxyanthranilate_3,4-dioxygenase 3-hydroxyanthranilate 3,4-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.6 1.13.11.6] </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=4hsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hsl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hsl RCSB], [http://www.ebi.ac.uk/pdbsum/4hsl PDBsum]</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=4hsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hsl OCA], [http://pdbe.org/4hsl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hsl RCSB], [http://www.ebi.ac.uk/pdbsum/4hsl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hsl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==

Revision as of 05:09, 5 August 2016

2.00 angstrom x-ray crystal structure of substrate-bound E110A 3-hydroxyanthranilate-3,4-dioxygenase from Cupriavidus metallidurans2.00 angstrom x-ray crystal structure of substrate-bound E110A 3-hydroxyanthranilate-3,4-dioxygenase from Cupriavidus metallidurans

Structural highlights

4hsl is a 1 chain structure with sequence from Cupriavidus metallidurans ch34. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:Cupriavidus metallidurans, nbaC, Rmet_5193 (Cupriavidus metallidurans CH34)
Activity:3-hydroxyanthranilate 3,4-dioxygenase, with EC number 1.13.11.6
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[3HAO_RALME] Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.[1]

References

  1. ↑ Colabroy KL, Zhai H, Li T, Ge Y, Zhang Y, Liu A, Ealick SE, McLafferty FW, Begley TP. The mechanism of inactivation of 3-hydroxyanthranilate-3,4-dioxygenase by 4-chloro-3-hydroxyanthranilate. Biochemistry. 2005 May 31;44(21):7623-31. PMID:15909977 doi:http://dx.doi.org/10.1021/bi0473455

4hsl, resolution 2.00Å

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