Structure of PDB 5ice Chain A

Receptor sequence
>5iceA (length=352) Species: 150095 (Thalictrum flavum subsp. glaucum) [Search protein sequence]
GAMVMINKENLSSQAKLWNFIYGFADSLVLKSAVQLDLANIIHNHGSPMT
LSELSLHLPSQPVNQDALYRVLRYLVHMKLFTKSSIDGELRYGLAPPAKF
LVKGWDKCMLGAILTITDKDFMAPWHYLKEGILNDGSTSTAFEKALGTNI
WDYMAEHPEKNQLFNEGMANDTRLIMSALVKECSSMFDGITTIVDVGGGT
GTAVRNIAKAFPHIKCTVYDLPHVIADSPGYTEINSIQGDMFKYIPNADA
IMMKCILHDWDDKECIEILKRCKDAVPRDGGKVIIIDIILDVKSEHPYTK
MRLTLDLDMMLNTGGKERTEEEWKKLIHDAGYKGYKITHISAVQSVIEAY
PY
3D structure
PDB5ice Crystal structure of norcoclaurine-6-O-methyltransferase, a key rate-limiting step in the synthesis of benzylisoquinoline alkaloids.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H256 D257 D285 E315
Catalytic site (residue number reindexed from 1) H258 D259 D287 E317
Enzyme Commision number 2.1.1.128: (RS)-norcoclaurine 6-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 W149 M166 T170 G195 D218 L219 D238 M239 K252 C253 I254 W151 M168 T172 G197 D220 L221 D240 M241 K254 C255 I256
BS02 2H4 A A110 I114 F162 G165 M166 D169 C253 H256 D257 D306 M307 N310 A112 I116 F164 G167 M168 D171 C255 H258 D259 D308 M309 N312
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008171 O-methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0030786 (RS)-norcoclaurine 6-O-methyltransferase activity
GO:0046983 protein dimerization activity
Biological Process
GO:0009820 alkaloid metabolic process
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:5ice, PDBe:5ice, PDBj:5ice
PDBsum5ice
PubMed27232113
UniProtQ5C9L7|6OMT_THLFG (RS)-norcoclaurine 6-O-methyltransferase

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