› 1kqo

X-ray diffraction
2.5Å resolution

Crystal structure of NMN/NaMN adenylyltransferase complexed with deamido-NAD

Released:
DOI: 10.2210/pdb1kqo/pdb
PDB entry 1kqo coloured by chain, front view.
PDB entry 1kqo coloured by chain, side view.
PDB entry 1kqo 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

1 bound ligand:
Ligand DND 6 x DND
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 131.245Å b: 90.391Å c: 137.673Å
α: 90° β: 117.17° γ: 90°
R-values:
R R work R free
0.21 0.21 0.246
Expression system: Escherichia coli

Quick links

Citations

15 review citations

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

3 mentions without citation

Homology modeling and deletion mutants of human nicotinamide mononucleotide adenylyltransferase isozyme 2: new insights on structure and function relationship.
Brunetti et al. (2010)
2 more