› 1m8f

X-ray diffraction
2.4Å resolution

Crystal Structure Of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase Mutant R11A complexed with NAD

Released:
DOI: 10.2210/pdb1m8f/pdb
PDB entry 1m8f coloured by chain, front view.
PDB entry 1m8f coloured by chain, side view.
PDB entry 1m8f coloured by chain, top view.
Source organism: Methanothermobacter thermautotrophicus
Primary publication:
Mutational, structural, and kinetic studies of the ATP-binding site of Methanobacterium thermoautotrophicum nicotinamide mononucleotide adenylyltransferase.
Saridakis V, Pai EF
J Biol Chem 278 34356-63 (2003)
PMID: 12810729

Function and Biology Details

Reaction catalysed: 
ATP + nicotinamide ribonucleotide = diphosphate + 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-127827 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nicotinamide-nucleotide adenylyltransferase Chain: A
Molecule details ›
Chain: A
Length: 181 amino acids
Theoretical weight: 20.48 KDa
Source organism: Methanothermobacter thermautotrophicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O26253 (Residues: 1-178; Coverage: 100%)
Gene name: MTH_150
Sequence domains: Cytidylyltransferase-like
Structure domains: HUPs

Ligands and Environments

1 bound ligand:
Ligand NAD 1 x NAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P6322
Unit cell:
a: 88.325Å b: 88.325Å c: 110.449Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.194 0.246
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme.
Zhai et al. (2009)
9 other articles

1 mention without citation

Phosphate binding sites identification in protein structures.
Parca et al. (2011)