Structure of PDB 5cvu Chain B

Receptor sequence
>5cvuB (length=360) Species: 36903 (Clarkia breweri) [Search protein sequence]
IQIIPTHSSDEEANLFAMQLASAAVLPMALKAAIELDVLEIMAKSVPPSG
YISPAEIAAQLPTTNPEAPVMLDRVLRLLASYSVVTYTLRELPSGKVERL
YGLAPVCKFLTKNEDGVSLAPFLLLATDKVLLEPWFYLKDAILEGGIPFN
KAYGMNIWDYFGTDHRINKVFNKGMSSNSTITMKKILEMYNGFEGLTTIV
DVGGGTGAVASMIVAKYPSINAINFDLPHVIQDAPAFSGVEHLGGDMFDG
VPKGDAIFIKWICHDWSDEHCLKLLKNCYAALPDHGKVIVAEYILPPSPD
PSIATKVVIHTDALMLAYNPGGKERTEKEFQALAMASGFRGFKVASCAFN
TYVMEFLKTA
3D structure
PDB5cvu Structure of sinapyl alcohol bound monolignol 4-O-methyltransferase at 1.60 Angstroms resolution
ChainB
Resolution1.8 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) H264 D265 E292 E324
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 55B B A134 W166 W269 H272 D273 L322 M323 Y326 N327 A126 W158 W261 H264 D265 L314 M315 Y318 N319
BS02 SAH B W166 M183 S187 G211 D234 L235 D254 M255 K268 I270 W158 M175 S179 G203 D226 L227 D246 M247 K260 I262
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5cvu, PDBe:5cvu, PDBj:5cvu
PDBsum5cvu
PubMed
UniProtO04385|IEMT_CLABR (Iso)eugenol O-methyltransferase (Gene Name=IEMT1)

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