Structure of PDB 5mzi Chain A Binding Site BS04

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 505 [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)		L427 F430 A431 N442 E449
Binding residue
(residue number reindexed from 1)		L418 F421 A422 N433 E440
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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