Structure of PDB 6lkd Chain A Binding Site BS02

Receptor Information
>6lkd Chain A (length=427) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TEGKRVVVIGGGLVGALNACFLAKRNFQVDVYEAREDIRVARSINLALSY
RGRQALKAVGLEDQIVSKGVPMKARMIHSLSGKKSAIPYGNKSQYILSIS
REKLNKDLLTAVESYPNAKVHFGHKLSKCLTMLGPNKVPRDITCDLIVGC
DGAYSTVRAHLMKKPRFDYSQQYIPHGYMELTIPPKNGEYAMEPNCLHIW
PRNAFMMIALPNMDKSFTCTLFMSFEEFEKLPTHSDVLDFFQKNFPDAIP
LMGEQALMRDFFLLPAQPMISVKCSPFHLKSRCVLMGDAAHAIVPFFGQG
MNAGFEDCLVFDELMDKFNNDLSVCLPEFSRFRIPDDHAISDLSMYNYIE
MRAHVNSRWFLFQRLLDKFLHALMPSTFIPLYTMVAFTRIRYHEAVLRWH
WQKKVINRGLFVLGSLVAIGSAYILVH
Ligand information
Ligand IDEGO
InChIInChI=1S/C24H18ClFN2O3/c1-15-13-27-28(23(15)17-7-9-20(25)21(26)11-17)18-8-10-22(19(12-18)24(29)30)31-14-16-5-3-2-4-6-16/h2-13H,14H2,1H3,(H,29,30)
InChIKeyNWWKXTLGLBRUHA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385Cc1cnn(c2ccc(OCc3ccccc3)c(c2)C(O)=O)c1c4ccc(Cl)c(F)c4
OpenEye OEToolkits 2.0.7Cc1cnn(c1c2ccc(c(c2)F)Cl)c3ccc(c(c3)C(=O)O)OCc4ccccc4
FormulaC24 H18 Cl F N2 O3
Name5-[5-(4-chloranyl-3-fluoranyl-phenyl)-4-methyl-pyrazol-1-yl]-2-phenylmethoxy-benzoic acid
ChEMBL
DrugBank
ZINC
PDB chain6lkd Chain A Residue 1002 [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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PDB6lkd Full-length in meso structure and mechanism of rat kynurenine 3-monooxygenase inhibition.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		R85 Y99 L213 I224 F238 F312 N363 M367 F376 Q379 R380 Y398
Binding residue
(residue number reindexed from 1)		R75 Y89 L197 I208 F222 F296 N347 M351 F360 Q363 R364 Y382
Annotation score1
Enzymatic activity
Enzyme Commision number 1.14.13.9: kynurenine 3-monooxygenase.
Gene Ontology
Molecular Function
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:0009651 response to salt stress
GO:0014049 positive regulation of glutamate secretion
GO:0019363 pyridine nucleotide biosynthetic process
GO:0019674 NAD metabolic process
GO:0019805 quinolinate biosynthetic process
GO:0032496 response to lipopolysaccharide
GO:0034276 kynurenic acid biosynthetic process
GO:0034354 'de novo' NAD biosynthetic process from tryptophan
GO:0043420 anthranilate metabolic process
GO:0070189 kynurenine metabolic process
GO:0071222 cellular response to lipopolysaccharide
GO:0071347 cellular response to interleukin-1
GO:0097052 L-kynurenine metabolic process
GO:1903296 positive regulation of glutamate secretion, neurotransmission
Cellular Component
GO:0005615 extracellular space
GO:0005739 mitochondrion
GO:0005741 mitochondrial outer membrane
GO:0031966 mitochondrial membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6lkd, PDBe:6lkd, PDBj:6lkd
PDBsum6lkd
PubMed33542467
UniProtO88867|KMO_RAT Kynurenine 3-monooxygenase (Gene Name=Kmo)

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