Structure of PDB 1yz3 Chain A

Receptor sequence
>1yz3A (length=263) Species: 9606 (Homo sapiens) [Search protein sequence]
PGQAAVASAYQRFEPRAYLRNNYAPPRGDLCNPNGVGPWKLRCLAQTFAT
GEVSGRTLIDIGSGPTVYQLLSACSHFEDITMTDFLEVNRQELGRWLQEE
PGAFNWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQPLGA
GSPAPLPADALVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGAL
EESWYLAGEARLTVVPVSEEEVREALVRSGYKVRDLRTYIMPAHLQTGVD
DVKGVFFAWAQKV
3D structure
PDB1yz3 Structural, mutagenic, and kinetic analysis of the binding of substrates and inhibitors of human phenylethanolamine N-methyltransferase
ChainA
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.1.1.28: phenylethanolamine N-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 SKA A Y35 N39 Y40 V53 K57 F182 E219 V269 Y18 N22 Y23 V36 K40 F165 E202 V252 MOAD: Ki=1.55nM
PDBbind-CN: -logKd/Ki=8.81,Ki=1.55nM
BindingDB: Ki=3.1nM,IC50=10nM
BS02 SAH A Y27 Y35 Y40 S80 T83 Y85 D101 F102 N106 D158 V159 A181 F182 C183 V187 Y10 Y18 Y23 S63 T66 Y68 D84 F85 N89 D141 V142 A164 F165 C166 V170
Gene Ontology
Molecular Function
GO:0004603 phenylethanolamine N-methyltransferase activity
GO:0005515 protein binding
GO:0008168 methyltransferase activity
Biological Process
GO:0032259 methylation
GO:0042418 epinephrine biosynthetic process
GO:0042423 catecholamine biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1yz3, PDBe:1yz3, PDBj:1yz3
PDBsum1yz3
PubMed16279783
UniProtP11086|PNMT_HUMAN Phenylethanolamine N-methyltransferase (Gene Name=PNMT)

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