› 2obf

X-ray diffraction
2.3Å resolution

Structure of K57A hPNMT with inhibitor 3-Hydroxymethyl-7-(N-4-chlorophenylaminosulfonyl)-THIQ and AdoHcy (SAH)

Released:
DOI: 10.2210/pdb2obf/pdb
PDB entry 2obf coloured by chain, front view.
PDB entry 2obf coloured by chain, side view.
PDB entry 2obf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Enzyme adaptation to inhibitor binding: a cryptic binding site in phenylethanolamine N-methyltransferase.
Gee CL, Drinkwater N, Tyndall JD, Grunewald GL, Wu Q, McLeish MJ, Martin JL
J Med Chem 50 4845-53 (2007)
PMID: 17845018

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 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: 31.79 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 F83 2 x F83
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P43212
Unit cell:
a: 94.68Å b: 94.68Å c: 188.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.267
Expression system: Escherichia coli

Quick links

Citations

10 citation in other articles

Equilibrium fluctuations of a single folded protein reveal a multitude of potential cryptic allosteric sites.
Bowman et al. (2012)
9 more

2 mentions without citation

A molecular mechanics approach to modeling protein-ligand interactions: relative binding affinities in congeneric series.
Rapp et al. (2011)
1 more