Structure of PDB 3reo Chain B

Receptor sequence
>3reoB (length=352) Species: 36903 (Clarkia breweri) [Search protein sequence]
SSDEEANLFAMQLASAAVLPMALKAAIELDVLEIMAKSVPPSGYISPAEI
AAQLPTTNPEAPVMLDRVLRLLASYSVVTYTLRELPSGKVERLYGLAPVC
KFLTKNEDGVSLAPFLLLATDKVLLEPWFYLKDAILEGGIPFNKAYGMNI
FDYHGTDHRINKVFNKGMSSNSTITMKKILEMYNGFEGLTTIVDVGGGTG
AVASMIVAKYPSINAINFDLPHVIQDAPAFSGVEHLGGDMFDGVPKGDAI
FIKWICHDWSDEHCLKLLKNCYAALPDHGKVIVAEYILPPSPDPSIATKV
VIHTDALMLAYNPGGKERTEKEFQALAMASGFRGFKVASCAFNTYVMEFL
KT
3D structure
PDB3reo Monolignol O-methyltransferase (MOMT)
ChainB
Resolution1.9 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) H257 D258 E285 E317
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 EUG B L133 A134 L139 I165 F166 F179 M183 D273 L322 Y326 N327 L118 A119 L124 I150 F151 F164 M168 D258 L307 Y311 N312
BS02 SAH B F166 F179 M183 S187 G211 D234 L235 D254 M255 F256 K268 I270 F151 F164 M168 S172 G196 D219 L220 D239 M240 F241 K253 I255
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:3reo, PDBe:3reo, PDBj:3reo
PDBsum3reo
PubMed
UniProtO04385|IEMT_CLABR (Iso)eugenol O-methyltransferase (Gene Name=IEMT1)

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