Structure of PDB 6fox Chain A Binding Site BS02

Receptor Information
>6fox Chain A (length=449) Species: 294 (Pseudomonas fluorescens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RQVTIIGAGLAGTLVARLLARNGWQVNLFERRPDPRIETGARGRSINLAL
AERGAHALRLAGLEREVLAEAVMMRGRMVHVPGTPPNLQPYGRDDSEVIW
SINRDRLNRILLDGAEAAGASIHFNLGLDSVDFARQRLTLSNVSGERLEK
RFHLLIGADGCNSAVRQAMASVVDLGEHLETQPHGYKELQITPEASAQFN
LEPNALHIWPHGDYMCIALPNLDRSFTVTLFLHHQSPAAQPASPSFAQLV
DGHAARRFFQRQFPDLSPMLDSLEQDFEHHPTGKLATLRLTTWHVGGQAV
LLGDAAHPMVPFHGQGMNCALEDAVALAEHLQSAADNASALAAFTAQRQP
DALAIQAMALENYVEMSSKVASPTYLLERELGQIMAQRQPTRFIPRYSMV
TFSRLPYAQAMARGQIQEQLLKFAVANHSDLTSINLDAVEHEVTRCLPP
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain6fox Chain A Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6fox A brain-permeable inhibitor of the neurodegenerative disease target kynurenine 3-monooxygenase prevents accumulation of neurotoxic metabolites.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		P318 G321 Q322 G323
Binding residue
(residue number reindexed from 1)		P311 G314 Q315 G316
Annotation score1
Enzymatic activity
Enzyme Commision number 1.14.13.9: kynurenine 3-monooxygenase.
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6fox, PDBe:6fox, PDBj:6fox
PDBsum6fox
PubMed31372510
UniProtQ84HF5|KMO_PSEFL Kynurenine 3-monooxygenase (Gene Name=kmo)

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