Structure of PDB 3reo Chain A

Receptor sequence
>3reoA (length=351) Species: 36903 (Clarkia breweri) [Search protein sequence]
SDEEANLFAMQLASAAVLPMALKAAIELDVLEIMAKSVPPSGYISPAEIA
AQLPTTNPEAPVMLDRVLRLLASYSVVTYTLRELPSGKVERLYGLAPVCK
FLTKNEDGVSLAPFLLLATDKVLLEPWFYLKDAILEGGIPFNKAYGMNIF
DYHGTDHRINKVFNKGMSSNSTITMKKILEMYNGFEGLTTIVDVGGGTGA
VASMIVAKYPSINAINFDLPHVIQDAPAFSGVEHLGGDMFDGVPKGDAIF
IKWICHDWSDEHCLKLLKNCYAALPDHGKVIVAEYILPPSPDPSIATKVV
IHTDALMLAYNPGGKERTEKEFQALAMASGFRGFKVASCAFNTYVMEFLK
T
3D structure
PDB3reo Monolignol O-methyltransferase (MOMT)
ChainA
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) H256 D257 E284 E316
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 A F166 F179 M183 S187 G211 D234 L235 D254 M255 F256 K268 I270 F150 F163 M167 S171 G195 D218 L219 D238 M239 F240 K252 I254
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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