Structure of PDB 5y77 Chain B

Receptor sequence
>5y77B (length=451) Species: 294 (Pseudomonas fluorescens) [Search protein sequence]
RQVTIIGAGLAGTLVARLLARNGWQVNLFERRPDPRIETGARGRSINLAL
AERGAHALRLAGLEREVLAEAVMMRGRMVHVPGTPPNLQPYGRDDSEVIW
SINRDRLNRILLDGAEAAGASIHFNLGLDSVDFARQRLTLSNVSGERLEK
RFHLLIGADGCNSAVRQAMASVVDLGEHLETQPHGYKELQITPEASAQFN
LEPNALHIWPHGDYMCIALPNLDRSFTVTLFLHHQSPAAQPASPCFAQLV
DGHAARRFFQRQFPDLSPMLDSLEQDFEHHPTGKLATLRLTTWHVGGQAV
LLGDAAHPMVPFHGQGMNCALEDAVALAEHLQSAADNASALAAFTAQRQP
DALAIQAMALENYVEMSSKVASPTYLLERELGQIMAQRQPTRFIPRYSMV
TFSRLPYAQAMARGQIQEQLLKFAVANHSDLTSINLDAVEHEVTRCLPPL
S
3D structure
PDB5y77 Biochemistry and structural studies of kynurenine 3-monooxygenase reveal allosteric inhibition by Ro 61-8048
ChainB
Resolution1.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.13.9: kynurenine 3-monooxygenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004497 monooxygenase activity
GO:0004502 kynurenine 3-monooxygenase activity
GO:0016174 NAD(P)H oxidase H2O2-forming activity
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
Biological Process
GO:0006569 tryptophan catabolic process
GO:0009435 NAD biosynthetic process
GO:0019363 pyridine nucleotide biosynthetic process
GO:0019674 NAD metabolic process
GO:0019805 quinolinate biosynthetic process
GO:0034354 'de novo' NAD biosynthetic process from tryptophan
GO:0043420 anthranilate metabolic process
GO:0070189 kynurenine metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5y77, PDBe:5y77, PDBj:5y77
PDBsum5y77
PubMed29208702
UniProtQ84HF5|KMO_PSEFL Kynurenine 3-monooxygenase (Gene Name=kmo)

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