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Structure paper

TitleFull-length in meso structure and mechanism of rat kynurenine 3-monooxygenase inhibition.
Journal, issue, pagesCommun Biol, Vol. 4, Page 159-159, Year 2021
Publish dateDec 19, 2019 (structure data deposition date)
AuthorsMimasu, S. / Yamagishi, H. / Kubo, S. / Kiyohara, M. / Matsuda, T. / Yahata, T. / Thomson, H.A. / Hupp, C.D. / Liu, J. / Okuda, T. / Kakefuda, K.
External linksCommun Biol / PubMed:33542467
MethodsX-ray diffraction
Resolution3 Å
Structure data

PDB-6lkd:
in meso full-length rat KMO in complex with a pyrazoyl benzoic acid inhibitor
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-6lke:
in meso full-length rat KMO in complex with an inhibitor identified via DNA-encoded chemical library screening
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-EGO:
5-[5-(4-chloranyl-3-fluoranyl-phenyl)-4-methyl-pyrazol-1-yl]-2-phenylmethoxy-benzoic acid

ChemComp-SO4:
SULFATE ION

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-EGU:
4-chloranyl-2-[[5-chloranyl-2-(5-methoxy-1,3-dihydroisoindol-2-yl)-1,3-thiazol-4-yl]carbonyl-methyl-amino]-5-fluoranyl-benzoic acid

Source
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / Single pass transmembrane / KMO / hydroxygenase / FLAVOPROTEIN / Single-pass transmembrane proteins / FAD

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