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==1.96 angstrom x-ray crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase bound with 3-aminosalicylic acid from cupraavidus metallidurans== | |||
<StructureSection load='4i3p' size='340' side='right' caption='[[4i3p]], [[Resolution|resolution]] 1.96Å' scene=''> | |||
== Structural highlights == | |||
==Function== | <table><tr><td colspan='2'>[[4i3p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cupriavidus_metallidurans_ch34 Cupriavidus metallidurans ch34]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I3P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I3P FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1CW:3-AMINO-2-HYDROXYBENZOIC+ACID'>1CW</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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='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=4i3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i3p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i3p RCSB], [http://www.ebi.ac.uk/pdbsum/4i3p PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/3HAO_RALME 3HAO_RALME]] Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.<ref>PMID:15909977</ref> | [[http://www.uniprot.org/uniprot/3HAO_RALME 3HAO_RALME]] Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.<ref>PMID:15909977</ref> | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
<references | |||
[[Category: 3-hydroxyanthranilate 3,4-dioxygenase]] | [[Category: 3-hydroxyanthranilate 3,4-dioxygenase]] | ||
[[Category: Liu, A | [[Category: Cupriavidus metallidurans ch34]] | ||
[[Category: Liu, F | [[Category: Liu, A]] | ||
[[Category: Liu, F]] | |||
[[Category: Bi-cupin iron-binding]] | [[Category: Bi-cupin iron-binding]] | ||
[[Category: Dioxygenase]] | [[Category: Dioxygenase]] | ||
[[Category: Oxioreductase-substrate complex]] | [[Category: Oxioreductase-substrate complex]] |
Revision as of 12:25, 25 December 2014
1.96 angstrom x-ray crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase bound with 3-aminosalicylic acid from cupraavidus metallidurans1.96 angstrom x-ray crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase bound with 3-aminosalicylic acid from cupraavidus metallidurans
Structural highlights
Function[3HAO_RALME] Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.[1] References
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