Structure of PDB 5nae Chain B Binding Site BS02

Receptor Information
>5nae Chain B (length=451) 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
PDALAIQAMALENYVEMSSKVASPTYLLERELGQIMAQRQPTRFIPRYSM
VTFSRLPYAQAMARGQIQEQLLKFAVANHSDLTSINLDAVEHEVTRCLPP
L
Ligand information
Ligand ID8R8
InChIInChI=1S/C17H15ClN2O5/c1-10(12-4-2-3-6-19-12)24-14-9-15-13(8-11(14)18)20(17(23)25-15)7-5-16(21)22/h2-4,6,8-10H,5,7H2,1H3,(H,21,22)/t10-/m1/s1
InChIKeyPVGOQRJICUIPTG-SNVBAGLBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.6CC(c1ccccn1)Oc2cc3c(cc2Cl)N(C(=O)O3)CCC(=O)O
CACTVS 3.385C[CH](Oc1cc2OC(=O)N(CCC(O)=O)c2cc1Cl)c3ccccn3
CACTVS 3.385C[C@@H](Oc1cc2OC(=O)N(CCC(O)=O)c2cc1Cl)c3ccccn3
OpenEye OEToolkits 2.0.6C[C@H](c1ccccn1)Oc2cc3c(cc2Cl)N(C(=O)O3)CCC(=O)O
FormulaC17 H15 Cl N2 O5
Name3-[5-chloranyl-2-oxidanylidene-6-[(1~{R})-1-pyridin-2-ylethoxy]-1,3-benzoxazol-3-yl]propanoic acid
ChEMBLCHEMBL4070212
DrugBank
ZINCZINC000473155182
PDB chain5nae Chain B Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5nae Structural and mechanistic basis of differentiated inhibitors of the acute pancreatitis target kynurenine-3-monooxygenase.
Resolution1.76 Å
Binding residue
(original residue number in PDB)		A56 R84 Y98 Y193 L213 I224 F238 P318 F319 G321 M373 Y404
Binding residue
(residue number reindexed from 1)		A50 R78 Y92 Y187 L207 I218 F232 P312 F313 G315 M367 Y398
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:5nae, PDBe:5nae, PDBj:5nae
PDBsum5nae
PubMed28604669
UniProtQ84HF5|KMO_PSEFL Kynurenine 3-monooxygenase (Gene Name=kmo)

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