Structure of PDB 3x0y Chain F

Receptor sequence
>3x0yF (length=400) Species: 1833 (Rhodococcus erythropolis) [Search protein sequence]
NDPVAVARGLAEKWRATAVERDRAGGSATAEREDLRASGLLSLLVPREYG
GWGADWPTAIEVVREIAAADGSLGHLFGYHLTNAPMIELIGSQEQEEHLY
TQIAQNNWWTGNASSENNSHVLDWKVRATPTEDGGYVLNGTKHFCSGAKG
SDLLFVFGVVQDDSPQQGAIIAAAIPTSRAGVTPNDDWAAIGMRQTDSGS
TDFHNVKVEPDEVLGAPNAFVLAFIQSERGSLFAPIAQLIFANVYLGIAH
GALDAAREYTRTQARPWTPAGIQQATEDPYTIRSYGEFTIALQGADAAAR
EAAHLLQTVWDKGDALTPEDRGELMVKVSGVKALATNAALNISSGVFEVI
GARGTHPRYGFDRFWRNVRTHSLHDPVSYKIADVGKHTLNGQYPIPGFTS
3D structure
PDB3x0y Crystal structures of apo-DszC and FMN-bound DszC from Rhodococcus erythropolis D-1.
ChainF
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S131 S132 E245 H404
Catalytic site (residue number reindexed from 1) S114 S115 E228 H387
Enzyme Commision number 1.14.14.21: dibenzothiophene 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 FMN F R282 G368 A369 R370 R265 G351 A352 R353
BS02 FMN F Y96 N129 N134 K159 F161 S163 H388 H391 Y79 N112 N117 K142 F144 S146 H371 H374
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004497 monooxygenase activity
GO:0008470 3-methylbutanoyl-CoA dehydrogenase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0006552 L-leucine catabolic process
GO:0018896 dibenzothiophene catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3x0y, PDBe:3x0y, PDBj:3x0y
PDBsum3x0y
PubMed25627402
UniProtA0A0C6DRW4|DSZC1_RHOER Dibenzothiophene monooxygenase (Gene Name=dszC)

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