Structure of PDB 5fn0 Chain B Binding Site BS02

Receptor Information
>5fn0 Chain B (length=455) Species: 294 (Pseudomonas fluorescens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NARQVTIIGAGLAGTLVARLLARNGWQVNLFERRPDPRIETGARGRSINL
ALAERGAHALRLAGLEREVLAEAVMMRGRMVHVPGTPPNLQPYGRDDSEV
IWSINRDRLNRILLDGAEAAGASIHFNLGLDSVDFARQRLTLSNVSGERL
EKRFHLLIGADGCNSAVRQAMASVVDLGEHLETQPHGYKELQITPEASAQ
FNLEPNALHIWPHGDYMCIALPNLDRSFTVTLFLHHQSPAAQPASPSFAQ
LVDGHAARRFFQRQFPDLSPMLDSLEQDFEHHPTGKLATLRLTTWHVGGQ
AVLLGDAAHPMVPFHGQGMNCALEDAVALAEHLQSAADNASALAAFTAQR
QPDALAIQAMALENYVEMSSKVASPTYLLERELGQIMAQRQPTRFIPRYS
MVTFSRLPYAQAMARGQIQEQLLKFAVANHSDLTSINLDAVEHEVTRCLP
PLSHL
Ligand information
Ligand IDJHY
InChIInChI=1S/C10H7Cl2NO4/c11-5-3-7-8(4-6(5)12)17-10(16)13(7)2-1-9(14)15/h3-4H,1-2H2,(H,14,15)
InChIKeyMIGAKMWKMLYGJX-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1c2c(cc(c1Cl)Cl)OC(=O)N2CCC(=O)O
CACTVS 3.385OC(=O)CCN1C(=O)Oc2cc(Cl)c(Cl)cc12
FormulaC10 H7 Cl2 N O4
Name3-(5,6-DICHLORO-2-OXOBENZO[D]OXAZOL-3(2H)-YL)PROPANOIC ACID
ChEMBLCHEMBL4092205
DrugBank
ZINC
PDB chain5fn0 Chain B Residue 4000 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5fn0 Kynurenine-3-Monooxygenase Inhibition Prevents Multiple Organ Failure in Rodent Models of Acute Pancreatitis.
Resolution3.19 Å
Binding residue
(original residue number in PDB)		R84 Y98 P318 F319 H320 G321 N369 M373
Binding residue
(residue number reindexed from 1)		R79 Y93 P313 F314 H315 G316 N364 M368
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:5fn0, PDBe:5fn0, PDBj:5fn0
PDBsum5fn0
PubMed26752518
UniProtQ84HF5|KMO_PSEFL Kynurenine 3-monooxygenase (Gene Name=kmo)

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