Structure of PDB 5cvv Chain B

Receptor sequence
>5cvvB (length=347) Species: 36903 (Clarkia breweri) [Search protein sequence]
SSDEEANLFAHQLARAASLPMALKAAIELDVLEIMAKSVPPSGYISPAEI
AAQLPTTNPEAPVMLDRVLRLLASYSVVTYTLRVERLYGLAPVCKFLTKN
EDGVSLAPFLLLATDKVLLEPWFYLKDAILEGGIPFNKAYGMNIWDYFGT
DHRINKVFNKGMSSNSTITMKKILEMYNGFEGLTTIVDVGGGTGAVASMI
VAKYPSINAINFDLPHVIQDAPAFSGVEHLGGDMFDGVPKGDAIFIKWIC
HDWSDEHCLKLLKNCYAALPDHGKVIVAEYILPPSPDPSIATKVVIHMDA
LMLAYNPGGKERTEKEFQALAMASGFRGFKVASCAFNTYVMEFLKTA
3D structure
PDB5cvv Structure of coniferyl alcohol bound monolignol 4-O-methyltransferase 9 at 1.73 Angstroms resolution
ChainB
Resolution1.73 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H272 D273 E300 E332
Catalytic site (residue number reindexed from 1) H251 D252 E279 E311
Enzyme Commision number 2.1.1.146: (iso)eugenol O-methyltransferase.
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 SAH B W166 F179 M183 S187 G211 D234 L235 D254 M255 K268 I270 W145 F158 M162 S166 G190 D213 L214 D233 M234 K247 I249
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008171 O-methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0046983 protein dimerization activity
GO:0050630 (iso)eugenol O-methyltransferase activity
Biological Process
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:5cvv, PDBe:5cvv, PDBj:5cvv
PDBsum5cvv
PubMed
UniProtO04385|IEMT_CLABR (Iso)eugenol O-methyltransferase (Gene Name=IEMT1)

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