› 6chh

X-ray diffraction
2.3Å resolution

Structure of human NNMT in complex with bisubstrate inhibitor MS2756

Released:
DOI: 10.2210/pdb6chh/pdb
PDB entry 6chh coloured by chain, front view.
PDB entry 6chh coloured by chain, side view.
PDB entry 6chh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery of Bisubstrate Inhibitors of Nicotinamide N-Methyltransferase (NNMT).
Babault N, Allali-Hassani A, Li F, Fan J, Yue A, Ju K, Liu F, Vedadi M, Liu J, Jin J
J Med Chem 61 1541-1551 (2018)
PMID: 29320176

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:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154068 (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

2 bound ligands:
Ligand F0P 4 x F0P
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P1
Unit cell:
a: 46.44Å b: 62.56Å c: 107.979Å
α: 91.76° β: 98.05° γ: 111.83°
R-values:
R R work R free
0.17 0.168 0.229
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Complex roles of nicotinamide N-methyltransferase in cancer progression.
Wang et al. (2022)
5 more

1 mention without citation

Bisubstrate Inhibitors of Nicotinamide N-Methyltransferase (NNMT) with Enhanced Activity.
Gao et al. (2019)