› 2an5

X-ray diffraction
2.5Å resolution

Structure of human PNMT complexed with S-adenosyl-homocysteine and an inhibitor, trans-(1S,2S)-2-amino-1-tetralol

Released:
DOI: 10.2210/pdb2an5/pdb
PDB entry 2an5 coloured by chain, front view.
PDB entry 2an5 coloured by chain, side view.
PDB entry 2an5 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

Assembly composition:
monomeric (preferred)
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
2 bound ligands:
Ligand TTL 2 x TTL
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P43212
Unit cell:
a: 94.02Å b: 94.02Å c: 187.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.246
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

4 mentions without citation

Conformational changes in redox pairs of protein structures.
Fan et al. (2009)
3 more