Structure of PDB 5nak Chain B

Receptor sequence
>5nakB (length=447) Species: 294 (Pseudomonas fluorescens) [Search protein sequence]
ARQVTIIGAGLAGTLVARLLARNGWQVNLFERRPDPRIETGARGRSINLA
LAERGAHALRLAGLEREVLAEAVMMRGRMVHVPGTPPNLQPYGRDDSEVI
WSINRDRLNRILLDGAEAAGASIHFNLGLDSVDFARQRLTLSNVSGERLE
KRFHLLIGADGCNSAVRQAMASVVDLGEHLETQPHGYKELQITPEASAQF
NLEPNALHIWPHGDYMCIALPNLDRSFTVTLFLHHQSPAAQPASPSFAQL
VDGHAARRFFQRQFPDLSPMLDSLEQDFEHHPTGKLATLRLTTWHVGGQA
VLLGDAAHPMVPFHGQGMNCALEDAVALAEHLQSAADNASALAAFTAQRQ
PDALAIQAMALENYVEMSSPTYLLERELGQIMAQRQPTRFIPRYSMVTFS
RLPYAQAMARGQIQEQLLKFAVANHSDLTSINLDAVEHEVTRCLPPL
3D structure
PDB5nak Structural and mechanistic basis of differentiated inhibitors of the acute pancreatitis target kynurenine-3-monooxygenase.
ChainB
Resolution1.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.13.9: kynurenine 3-monooxygenase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 FAD B I13 L17 A18 E37 R38 L55 A56 R111 G134 L135 D166 Y193 D311 P318 G321 Q322 G323 M324 N325 I7 L11 A12 E31 R32 L49 A50 R105 G128 L129 D160 Y187 D305 P312 G315 Q316 G317 M318 N319
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

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Molecular Function

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Biological Process
External links
PDB RCSB:5nak, PDBe:5nak, PDBj:5nak
PDBsum5nak
PubMed28604669
UniProtQ84HF5|KMO_PSEFL Kynurenine 3-monooxygenase (Gene Name=kmo)

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