Structure of PDB 5cvu Chain D

Receptor sequence
>5cvuD (length=361) Species: 36903 (Clarkia breweri) [Search protein sequence]
EIQIIPTHSSDEEANLFAMQLASAAVLPMALKAAIELDVLEIMAKSVPPS
GYISPAEIAAQLPTTNPEAPVMLDRVLRLLASYSVVTYTLRELPSGKVER
LYGLAPVCKFLTKNEDGVSLAPFLLLATDKVLLEPWFYLKDAILEGGIPF
NKAYGMNIWDYFGTDHRINKVFNKGMSSNSTITMKKILEMYNGFEGLTTI
VDVGGGTGAVASMIVAKYPSINAINFDLPHVIQDAPAFSGVEHLGGDMFD
GVPKGDAIFIKWICHDWSDEHCLKLLKNCYAALPDHGKVIVAEYILPPSP
DPSIATKVVIHTDALMLAYNPGGKERTEKEFQALAMASGFRGFKVASCAF
NTYVMEFLKTA
3D structure
PDB5cvu Structure of sinapyl alcohol bound monolignol 4-O-methyltransferase at 1.60 Angstroms resolution
ChainD
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) H265 D266 E293 E325
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 D F130 A134 W166 W269 H272 D273 N327 F123 A127 W159 W262 H265 D266 N320
BS02 SAH D W166 M183 S187 G211 D234 L235 D254 M255 K268 I270 W159 M176 S180 G204 D227 L228 D247 M248 K261 I263
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:5cvu, PDBe:5cvu, PDBj:5cvu
PDBsum5cvu
PubMed
UniProtO04385|IEMT_CLABR (Iso)eugenol O-methyltransferase (Gene Name=IEMT1)

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