› 3rod

X-ray diffraction
2.72Å resolution

Methyltransferase

Released:
DOI: 10.2210/pdb3rod/pdb
PDB entry 3rod coloured by chain, front view.
PDB entry 3rod coloured by chain, side view.
PDB entry 3rod coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of substrate recognition in human nicotinamide N-methyltransferase.
Peng Y, Sartini D, Pozzi V, Wilk D, Emanuelli M, Yee VC
Biochemistry 50 7800-8 (2011)
PMID: 21823666

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + nicotinamide = S-adenosyl-L-homocysteine + 1-methylnicotinamide
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154063 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nicotinamide N-methyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 283 amino acids
Theoretical weight: 31.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P40261 (Residues: 1-264; Coverage: 100%)
Gene name: NNMT
Sequence domains: NNMT/PNMT/TEMT family
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 4 x SAH
1 bound ligand:
Ligand NCA 4 x NCA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 60.663Å b: 61.793Å c: 74.342Å
α: 106.57° β: 103.98° γ: 104.14°
R-values:
R R work R free
0.208 0.205 0.264
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Architectures, mechanisms and molecular evolution of natural product methyltransferases.
Liscombe et al. (2012)
8 more

17 mentions without citation

Mechanisms and inhibitors of nicotinamide N-methyltransferase.
Iyamu et al. (2021)
16 more