Structure of PDB 5mzi Chain A Binding Site BS02

Receptor Information
>5mzi Chain A (length=448) Species: 294 (Pseudomonas fluorescens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ARQVTIIGAGLAGTLVARLLARNGWQVNLFERRPDPRIETGARGRSINLA
LAERGAHALRLAGLEREVLAEAVMMRGRMVHVPGTPPNLQPYGRDDSEVI
WSINRDRLNRILLDGAEAAGASIHFNLGLDSVDFARQRLTLSNVSGERLE
KRFHLLIGADGCNSAVRQAMASVVDLGEHLETQPHGYKELQITPEASAQF
NLEPNALHIWPHGDYMCIALPNLDRSFTVTLFLHHQSPAAQPASPSFAQL
VDGHAARRFFQRQFPDLSPMLDSLEQDFEHHPTGKLATLRLTTWHVGGQA
VLLGDAAHPMVPFHGQGMNCALEDAVALAEHLQSAADNASALAAFTAQRQ
PDALAIQAMALENYVEMSSSPTYLLERELGQIMAQRQPTRFIPRYSMVTF
SRLPYAQAMARGQIQEQLLKFAVANHSDLTSINLDAVEHEVTRCLPPL
Ligand information
Ligand IDFYK
InChIInChI=1S/C13H12ClNO5/c14-8-5-9-11(6-10(8)19-7-1-2-7)20-13(18)15(9)4-3-12(16)17/h5-7H,1-4H2,(H,16,17)
InChIKeyAYXQPTCYJAJHBG-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385OC(=O)CCN1C(=O)Oc2cc(OC3CC3)c(Cl)cc12
OpenEye OEToolkits 2.0.6c1c2c(cc(c1Cl)OC3CC3)OC(=O)N2CCC(=O)O
FormulaC13 H12 Cl N O5
Name3-(5-chloro-6-cyclopropoxy-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
ChEMBLCHEMBL4061542
DrugBank
ZINC
PDB chain5mzi Chain A Residue 503 [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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PDB5mzi Development of a Series of Kynurenine 3-Monooxygenase Inhibitors Leading to a Clinical Candidate for the Treatment of Acute Pancreatitis.
Resolution1.71 Å
Binding residue
(original residue number in PDB)		R84 I224 F238 P318 F319 H320 G321 N369 M373
Binding residue
(residue number reindexed from 1)		R78 I218 F232 P312 F313 H314 G315 N363 M367
Annotation score1
Binding affinityMOAD: ic50=3.162nM
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:5mzi, PDBe:5mzi, PDBj:5mzi
PDBsum5mzi
PubMed28398044
UniProtQ84HF5|KMO_PSEFL Kynurenine 3-monooxygenase (Gene Name=kmo)

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