› 1hlw

X-ray diffraction
1.9Å resolution

STRUCTURE OF THE H122A MUTANT OF THE NUCLEOSIDE DIPHOSPHATE KINASE

Released:
DOI: 10.2210/pdb1hlw/pdb
PDB entry 1hlw coloured by chain, front view.
PDB entry 1hlw coloured by chain, side view.
PDB entry 1hlw coloured by chain, top view.
Source organism: Dictyostelium discoideum
Primary publication:
Chemical rescue of phosphoryl transfer in a cavity mutant: a cautionary tale for site-directed mutagenesis.
Admiraal SJ, Meyer P, Schneider B, Deville-Bonne D, Janin J, Herschlag D
Biochemistry 40 403-13 (2001)
PMID: 11148034

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: 16.75 KDa
Source organism: Dictyostelium discoideum
Expression system: Escherichia coli
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
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P6322
Unit cell:
a: 75.001Å b: 75.001Å c: 106.169Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.166 0.208
Expression system: Escherichia coli

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Citations

2 review citations

A twisted base? The role of arginine in enzyme-catalyzed proton abstractions.
Guillén Schlippe et al. (2005)
1 more