4wlj: Difference between revisions

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<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=4wlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wlj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wlj RCSB], [http://www.ebi.ac.uk/pdbsum/4wlj 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=4wlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wlj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wlj RCSB], [http://www.ebi.ac.uk/pdbsum/4wlj PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/KAT1_HUMAN KAT1_HUMAN]] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.<ref>PMID:19338303</ref> 
== References ==
<references/>
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</StructureSection>
</StructureSection>

Revision as of 20:05, 25 December 2014

High resolution crystal structure of human kynurenine aminotransferase-I in complex with aminooxyacetateHigh resolution crystal structure of human kynurenine aminotransferase-I in complex with aminooxyacetate

Structural highlights

4wlj is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[KAT1_HUMAN] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.[1]

References

  1. ↑ Han Q, Robinson H, Cai T, Tagle DA, Li J. Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K. J Med Chem. 2009 May 14;52(9):2786-93. PMID:19338303 doi:10.1021/jm9000874

4wlj, resolution 1.54Å

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