› 3zto

X-ray diffraction
1.47Å resolution

Orthorhombic crystal form C222 of the Aquifex aeolicus nucleoside diphosphate kinase

Released:
DOI: 10.2210/pdb3zto/pdb
PDB entry 3zto coloured by chain, front view.
PDB entry 3zto coloured by chain, side view.
PDB entry 3zto coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
An intersubunit disulfide bridge stabilizes the tetrameric nucleoside diphosphate kinase of Aquifex aeolicus.
Boissier F, Georgescauld F, Moynié L, Dupuy JW, Sarger C, Podar M, Lascu I, Giraud MF, Dautant A
Proteins 80 1658-68 (2012)
PMID: 22467275

Function and Biology Details

Reaction catalysed: 
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130509 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nucleoside diphosphate kinase Chain: A
Molecule details ›
Chain: A
Length: 142 amino acids
Theoretical weight: 15.96 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O67528 (Residues: 1-142; Coverage: 100%)
Gene names: aq_1590, ndk
Sequence domains: Nucleoside diphosphate kinase
Structure domains: Nucleoside diphosphate kinase-like domain

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: C222
Unit cell:
a: 43.13Å b: 101.06Å c: 62.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.152 0.151 0.181
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Structure, Folding and Stability of Nucleoside Diphosphate Kinases.
Georgescauld et al. (2020)
4 other articles

1 mention without citation

A Homozygous Nme7 Mutation Is Associated with Situs Inversus Totalis.
Reish et al. (2016)