Structure of PDB 3fmw Chain C

Receptor sequence
>3fmwC (length=489) Species: 41951 (Streptomyces argillaceus) [Search protein sequence]
TTDVVVVGGGPVGLMLAGELRAGGVGALVLEKLVEPVGHDRAGALHIRTV
ETLDLRGLLDRFLEGTQVAKGLPFAGIFTQGLDFGLVDTRHPYTGLVPQS
RTEALLAEHAREAGAEIPRGHEVTRLRQDAEAVEVTVAGPSGPYPVRARY
GVGCDGGRSTVRRLAADRFPGTEATVRALIGYVTTPEREVPRRWERTPDG
ILVLAFPPGWSSSSTGHSDEGPVTLEDLGAAVARVRGTPLTLTEPVSWLS
RFGDASRQAKRYRSGRVLLAGDAAHVHFPIGGQGLNTGLQDAVNLGWKLA
ARVRGWGSEELLDTYHDERHPVAERVLLNTRAQLALMRPDEQHTTPLRGF
VEELLGTDEVNRYFTGMITGTDVRYATFAPASARPHPWPGRFAGGLVLSR
PSGEPVPVAELLRSARPLLLDLAGRADLREATRPWSDRVSVVAGEATVEP
PAQALLVRPDGYVAWAGSPAATADELRASLARWFGPPAN
3D structure
PDB3fmw Crystal structure of Baeyer-Villiger monooxygenase MtmOIV, the key enzyme of the mithramycin biosynthetic pathway .
ChainC
Resolution2.89 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G54 A80 P219 W227 P299
Catalytic site (residue number reindexed from 1) G43 A69 P208 W210 P279
Enzyme Commision number ?
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 C V18 G19 G21 P22 V23 E42 K43 R52 G54 A55 Q110 D166 G167 T171 F272 D292 P299 G302 G304 L305 N306 V7 G8 G10 P11 V12 E31 K32 R41 G43 A44 Q99 D155 G156 T160 F252 D272 P279 G282 G284 L285 N286
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0016709 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
GO:0071949 FAD binding

View graph for
Molecular Function
External links
PDB RCSB:3fmw, PDBe:3fmw, PDBj:3fmw
PDBsum3fmw
PubMed19364090
UniProtQ194P4

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