Structure of PDB 3p9i Chain D

Receptor sequence
>3p9iD (length=351) Species: 4522 (Lolium perenne) [Search protein sequence]
ASADEDACMFALQLASSSVLPMTLKNAIELGLLEILVAAGGKSLTPTEVA
AKLPSAANPEAPDMVDRILRLLASYNVVTCLVEEGKDGRLSRSYGAAPVC
KFLTPNEDGVSMAALALMNQDKVLMESWYYLKDAVLDGGIPFNKAYGMSA
FEYHGTDPRFNRVFNEGMKNHSIIITKKLLELYHGFEGLGTLVDVGGGVG
ATVAAIAAHYPTIKGVNFDLPHVISEAPQFPGVTHVGGDMFKEVPSGDTI
LMKWILHDWSDQHCATLLKNCYDALPAHGKVVLVQCILPVNPEANPSSQG
VFHVDMIMLAHNPGGRERYEREFQALARGAGFTGVKSTYIYANAWAIEFT
K
3D structure
PDB3p9i Structure-Function Analyses of a Caffeic Acid O-Methyltransferase from Perennial Ryegrass Reveal the Molecular Basis for Substrate Preference.
ChainD
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H266 D267 Q294 E326
Catalytic site (residue number reindexed from 1) H257 D258 Q285 E317
Enzyme Commision number 2.1.1.6: catechol 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 D F160 F173 M177 S181 G205 D228 L229 D248 M249 K262 F151 F164 M168 S172 G196 D219 L220 D239 M240 K253
BS02 SNY D M127 M177 W263 H266 D267 M317 M118 M168 W254 H257 D258 M308
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008171 O-methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0016206 catechol O-methyltransferase activity
GO:0046983 protein dimerization activity
Biological Process
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:3p9i, PDBe:3p9i, PDBj:3p9i
PDBsum3p9i
PubMed21177481
UniProtQ9ZTU2

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