› 2an3

X-ray diffraction
2.2Å resolution

Structure of PNMT with S-adenosyl-L-homocysteine and the semi-rigid analogue acceptor substrate cis-(1R,2S)-2-amino-1-tetralol.

Released:
DOI: 10.2210/pdb2an3/pdb
PDB entry 2an3 coloured by chain, front view.
PDB entry 2an3 coloured by chain, side view.
PDB entry 2an3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mode of binding of methyl acceptor substrates to the adrenaline-synthesizing enzyme phenylethanolamine N-methyltransferase: implications for catalysis.
Gee CL, Tyndall JD, Grunewald GL, Wu Q, McLeish MJ, Martin JL
Biochemistry 44 16875-85 (2005)
PMID: 16363801

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L-homocysteine + N-methylphenylethanolamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-145654 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylethanolamine N-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 289 amino acids
Theoretical weight: 31.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11086 (Residues: 1-282; Coverage: 100%)
Gene names: PENT, PNMT
Sequence domains: NNMT/PNMT/TEMT family
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
1 bound ligand:
Ligand CTL 2 x CTL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P43212
Unit cell:
a: 93.78Å b: 93.78Å c: 187.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.256
Expression system: Escherichia coli

Quick links

Citations

13 citation in other articles

Structural basis of substrate recognition in human nicotinamide N-methyltransferase.
Peng et al. (2011)
12 more

1 mention without citation

Binding mode information improves fragment docking.
Jacquemard et al. (2019)