Structure of PDB 3p9k Chain C

Receptor sequence
>3p9kC (length=357) Species: 4522 (Lolium perenne) [Search protein sequence]
TAADMAASADEDACMFALQLASSSVLPMTLKNAIELGLLEILVAAGGKSL
TPTEVAAKLPSAANPEAPDMVDRILRLLASYNVVTCLVEEGKDGRLSRSY
GAAPVCKFLTPNEDGVSMAALALMNQDKVLMESWYYLKDAVLDGGIPFNK
AYGMSAFEYHGTDPRFNRVFNEGMKNHSIIITKKLLELYHGFEGLGTLVD
VGGGVGATVAAIAAHYPTIKGVNFDLPHVISEAPQFPGVTHVGGDMFKEV
PSGDTILMKWILHDWSDQHCATLLKNCYDALPAHGKVVLVQCILPVNPEA
NPSSQGVFHVDMIMLAHNPGGRERYEREFQALARGAGFTGVKSTYIYANA
WAIEFTK
3D structure
PDB3p9k Structure-Function Analyses of a Caffeic Acid O-Methyltransferase from Perennial Ryegrass Reveal the Molecular Basis for Substrate Preference.
ChainC
Resolution2.25 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) H263 D264 Q291 E323
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 C F160 M177 S181 G205 D228 L229 D248 M249 K262 I264 F157 M174 S178 G202 D225 L226 D245 M246 K259 I261
BS02 CIY C M127 N128 W263 H266 D267 M317 M124 N125 W260 H263 D264 M314
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:3p9k, PDBe:3p9k, PDBj:3p9k
PDBsum3p9k
PubMed21177481
UniProtQ9ZTU2

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