› 1k4k

X-ray diffraction
2Å resolution

Crystal structure of E. coli Nicotinic acid mononucleotide adenylyltransferase

Released:
DOI: 10.2210/pdb1k4k/pdb
PDB entry 1k4k coloured by chain, front view.
PDB entry 1k4k coloured by chain, side view.
PDB entry 1k4k coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD.
Zhang H, Zhou T, Kurnasov O, Cheek S, Grishin NV, Osterman A
Structure 10 69-79 (2002)
PMID: 11796112

Function and Biology Details

Reaction catalysed: 
ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD(+)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141535 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nicotinate-nucleotide adenylyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 213 amino acids
Theoretical weight: 24.55 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A752 (Residues: 1-213; Coverage: 100%)
Gene names: JW0634, b0639, nadD, ybeN
Sequence domains: Cytidylyltransferase-like
Structure domains: HUPs

Ligands and Environments

1 bound ligand:
Ligand XE 4 x XE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300, APS BEAMLINE 19-BM
Spacegroup: P1
Unit cell:
a: 58.435Å b: 66.528Å c: 72.855Å
α: 72.68° β: 88.77° γ: 69.55°
R-values:
R R work R free
0.21 0.21 0.262
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Microbial NAD metabolism: lessons from comparative genomics.
Gazzaniga et al. (2009)
5 more

4 mentions without citation

Isoform-specific targeting and interaction domains in human nicotinamide mononucleotide adenylyltransferases.
Lau et al. (2010)
3 more