› 1nsp

X-ray diffraction
2.1Å resolution

MECHANISM OF PHOSPHATE TRANSFER BY NUCLEOSIDE DIPHOSPHATE KINASE: X-RAY STRUCTURES OF A PHOSPHO-HISTIDINE INTERMEDIATE OF THE ENZYMES FROM DROSOPHILA AND DICTYOSTELIUM

Released:
DOI: 10.2210/pdb1nsp/pdb
PDB entry 1nsp coloured by chain, front view.
PDB entry 1nsp coloured by chain, side view.
PDB entry 1nsp coloured by chain, top view.
Source organism: Dictyostelium discoideum
Primary publication:
Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium.
Moréra S, Chiadmi M, LeBras G, Lascu I, Janin J
Biochemistry 34 11062-70 (1995)
PMID: 7669763

Function and Biology Details

Reaction catalysed: 
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
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-149819 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nucleoside diphosphate kinase, cytosolic Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 16.9 KDa
Source organism: Dictyostelium discoideum
Expression system: Not provided
UniProt:
  • Canonical: P22887 (Residues: 1-155; Coverage: 100%)
Gene names: DDB_G0273069, DDB_G0273805, gip17, ndkB, ndkC-1, ndkC-2
Sequence domains: Nucleoside diphosphate kinase
Structure domains: Nucleoside diphosphate kinase-like domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand HIP 1 x HIP

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6322
Unit cell:
a: 75.16Å b: 75.16Å c: 105.93Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 not available
Expression system: Not provided

Quick links

Citations

18 review citations

Two-component signal transduction.
Stock et al. (2000)
17 more

7 mentions without citation

The many ways that nature has exploited the unusual structural and chemical properties of phosphohistidine for use in proteins.
Kalagiri et al. (2021)
6 more