› 1kqn

X-ray diffraction
2.2Å resolution

Crystal structure of NMN/NaMN adenylyltransferase complexed with NAD

Released:
DOI: 10.2210/pdb1kqn/pdb
PDB entry 1kqn coloured by chain, front view.
PDB entry 1kqn coloured by chain, side view.
PDB entry 1kqn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin.
Zhou T, Kurnasov O, Tomchick DR, Binns DD, Grishin NV, Marquez VE, Osterman AL, Zhang H
J Biol Chem 277 13148-54 (2002)
PMID: 11788603

Function and Biology Details

Reactions catalysed: 
ATP + nicotinamide ribonucleotide = diphosphate + NAD(+)
ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190716 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 279 amino acids
Theoretical weight: 31.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HAN9 (Residues: 1-279; Coverage: 100%)
Gene names: NMNAT, NMNAT1
Sequence domains: Cytidylyltransferase-like
Structure domains: HUPs

Ligands and Environments

2 bound ligands:
Ligand NAD 6 x NAD
Ligand XE 15 x XE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P21
Unit cell:
a: 130.816Å b: 90.879Å c: 136.585Å
α: 90° β: 116.85° γ: 90°
R-values:
R R work R free
0.218 0.218 0.25
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence.
Rajman et al. (2018)
12 more

8 mentions without citation

New facets in the regulation of gene expression by ADP-ribosylation and poly(ADP-ribose) polymerases.
Ryu et al. (2015)
7 more