Structure of PDB 1hnn Chain A

Receptor sequence

>1hnnA (length=261) Species: 9606 (Homo sapiens)

AVASAYQRFEPRAYLRNNYAPPRGDLCNPNGVGPWKLRCLAQTFATGEVS
GRTLIDIGSGPTVYQLLSACSHFEDITMTDFLEVNRQELGRWLQEEPGAF
NWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQPLGAGSPA
PLPADALVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESW
YLAGEARLTVVPVSEEEVREALVRSGYKVRDLRTYIMPAHLQTGVDDVKG
VFFAWAQKVGL

3D structure

• PDB: 1hnn Getting the adrenaline going: crystal structure of the adrenaline-synthesizing enzyme PNMT.
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E185 E219
• Catalytic site (residue number reindexed from 1): E164 E198
• 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	SAH	A	Y27 Y35 Y40 S80 G81 T83 Y85 D101 F102 L103 N106 D158 V159 H160 A181 F182 C183 V187	Y6 Y14 Y19 S59 G60 T62 Y64 D80 F81 L82 N85 D137 V138 H139 A160 F161 C162 V166
BS02	SKF	A	Y35 N39 Y40 R44 V53 K57 F182 E219 M258	Y14 N18 Y19 R23 V32 K36 F161 E198 M237	MOAD: Ki=0.58uM PDBbind-CN: -logKd/Ki=6.24,Ki=0.58uM BindingDB: Ki=280nM

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

External links

• PDB: RCSB:1hnn, PDBe:1hnn, PDBj:1hnn
• PDBsum: 1hnn
• PubMed: 11591352
• UniProt: P11086|PNMT_HUMAN Phenylethanolamine N-methyltransferase (Gene Name=PNMT)