Structure of PDB 3tky Chain A

Receptor sequence
>3tkyA (length=352) Species: 36903 (Clarkia breweri) [Search protein sequence]
SSDEEANLFAMQLASAAVLPMALKAAIELDVLEIMAKSVPPSGYISPAEI
AAQLPTTNPEAPVMLDRVLRLLASYSVVTYTLRELPSGKVERLYGLAPVC
KFLTKNEDGVSLAPFLLLATDKVLLEPWFYLKDAILEGGIPFNKAYGMNI
FDYHGTDHRINKVFNKGMSSNSTITMKKILEMYNGFEGLTTIVDVGGGTG
AVASMIVAKYPSINAINFDLPHVIQDAPAFSGVEHLGGDMFDGVPKGDAI
FIKWICHDWSDEHCLKLLKNCYAALPDHGKVIVAEYILPPSPDPSIATKV
VIHTDALMLAYNPGGKERTEKEFQALAMASGFRGFKVASCAFNTYVMEFL
KT
3D structure
PDB3tky An engineered monolignol 4-o-methyltransferase depresses lignin biosynthesis and confers novel metabolic capability in Arabidopsis.
ChainA
Resolution2.47 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 N7I A I165 F166 F179 D273 M323 Y326 N327 I150 F151 F164 D258 M308 Y311 N312
BS02 SAH A F166 G211 G212 D234 L235 D254 M255 F256 K268 I270 F151 G196 G197 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
View graph for
Biological Process
External links
PDB RCSB:3tky, PDBe:3tky, PDBj:3tky
PDBsum3tky
PubMed22851762
UniProtO04385|IEMT_CLABR (Iso)eugenol O-methyltransferase (Gene Name=IEMT1)

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