Structure of PDB 3p9i Chain B

Receptor sequence
>3p9iB (length=356) Species: 4522 (Lolium perenne) [Search protein sequence]
AADMAASADEDACMFALQLASSSVLPMTLKNAIELGLLEILVAAGGKSLT
PTEVAAKLPSAANPEAPDMVDRILRLLASYNVVTCLVEEGKDGRLSRSYG
AAPVCKFLTPNEDGVSMAALALMNQDKVLMESWYYLKDAVLDGGIPFNKA
YGMSAFEYHGTDPRFNRVFNEGMKNHSIIITKKLLELYHGFEGLGTLVDV
GGGVGATVAAIAAHYPTIKGVNFDLPHVISEAPQFPGVTHVGGDMFKEVP
SGDTILMKWILHDWSDQHCATLLKNCYDALPAHGKVVLVQCILPVNPEAN
PSSQGVFHVDMIMLAHNPGGRERYEREFQALARGAGFTGVKSTYIYANAW
AIEFTK
3D structure
PDB3p9i Structure-Function Analyses of a Caffeic Acid O-Methyltransferase from Perennial Ryegrass Reveal the Molecular Basis for Substrate Preference.
ChainB
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) H262 D263 Q290 E322
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 B F160 F173 M177 S181 G205 D228 L229 D248 M249 K262 I264 F156 F169 M173 S177 G201 D224 L225 D244 M245 K258 I260
BS02 SNY B M127 N128 M177 W263 H266 D267 M317 M123 N124 M173 W259 H262 D263 M313
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
View graph for
Biological Process
External links
PDB RCSB:3p9i, PDBe:3p9i, PDBj:3p9i
PDBsum3p9i
PubMed21177481
UniProtQ9ZTU2

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