Structure of PDB 1yz3 Chain B

Receptor sequence
>1yz3B (length=267) Species: 9606 (Homo sapiens) [Search protein sequence]
PDSAPGQAAVASAYQRFEPRAYLRNNYAPPRGDLCNPNGVGPWKLRCLAQ
TFATGEVSGRTLIDIGSGPTVYQLLSACSHFEDITMTDFLEVNRQELGRW
LQEEPGAFNWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQ
PLGAGSPAPLPADALVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLL
IGALEESWYLAGEARLTVVPVSEEEVREALVRSGYKVRDLRTYIMPAHLQ
TGVDDVKGVFFAWAQKV
3D structure
PDB1yz3 Structural, mutagenic, and kinetic analysis of the binding of substrates and inhibitors of human phenylethanolamine N-methyltransferase
ChainB
Resolution2.4 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 B Y35 N39 Y40 V53 F182 E219 D267 Y22 N26 Y27 V40 F169 E206 D254 MOAD: Ki=1.55nM
BindingDB: Ki=3.1nM,IC50=10nM
BS02 SAH B Y27 Y35 Y40 S80 T83 Y85 D101 F102 L103 N106 D158 V159 A181 F182 C183 V187 Y14 Y22 Y27 S67 T70 Y72 D88 F89 L90 N93 D145 V146 A168 F169 C170 V174
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1yz3, PDBe:1yz3, PDBj:1yz3
PDBsum1yz3
PubMed16279783
UniProtP11086|PNMT_HUMAN Phenylethanolamine N-methyltransferase (Gene Name=PNMT)

[Back to BioLiP]