Structure of PDB 5mzc Chain A Binding Site BS04

Receptor Information
>5mzc 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 ID8EQ
InChIInChI=1S/C12H12ClNO5/c1-2-18-9-6-10-8(5-7(9)13)14(12(17)19-10)4-3-11(15)16/h5-6H,2-4H2,1H3,(H,15,16)
InChIKeyKPOKXAQERBEAHE-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.6CCOc1cc2c(cc1Cl)N(C(=O)O2)CCC(=O)O
CACTVS 3.385CCOc1cc2OC(=O)N(CCC(O)=O)c2cc1Cl
FormulaC12 H12 Cl N O5
Name3-(5-chloranyl-6-ethoxy-2-oxidanylidene-1,3-benzoxazol-3-yl)propanoic acid
ChEMBLCHEMBL4072922
DrugBank
ZINC
PDB chain5mzc Chain A Residue 505 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5mzc Development of a Series of Kynurenine 3-Monooxygenase Inhibitors Leading to a Clinical Candidate for the Treatment of Acute Pancreatitis.
Resolution1.82 Å
Binding residue
(original residue number in PDB)		L427 F430 A431 E449
Binding residue
(residue number reindexed from 1)		L418 F421 A422 E440
Annotation score1
Binding affinityMOAD: ic50=5.012nM
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:5mzc, PDBe:5mzc, PDBj:5mzc
PDBsum5mzc
PubMed28398044
UniProtQ84HF5|KMO_PSEFL Kynurenine 3-monooxygenase (Gene Name=kmo)

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