› 3pnq

X-ray diffraction
2.2Å resolution

Crystal Structure of E.coli Dha kinase DhaK (H56N) complex with Dha

Released:
DOI: 10.2210/pdb3pnq/pdb
PDB entry 3pnq coloured by chain, front view.
PDB entry 3pnq coloured by chain, side view.
PDB entry 3pnq coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural and mechanistic insight into covalent substrate binding by Escherichia coli dihydroxyacetone kinase.
Shi R, McDonald L, Cui Q, Matte A, Cygler M, Ekiel I
Proc Natl Acad Sci U S A 108 1302-7 (2011)
PMID: 21209328

Function and Biology Details

Reaction catalysed: 
Phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160035 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PEP-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 357 amino acids
Theoretical weight: 38.24 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P76015 (Residues: 2-356; Coverage: 100%)
Gene names: JW5187, b1200, dhaK, ycgT
Sequence domains: Dak1 domain
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P21
Unit cell:
a: 82.232Å b: 101.073Å c: 99.349Å
α: 90° β: 89.95° γ: 90°
R-values:
R R work R free
0.2 0.2 0.22
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Regulation of histone gene expression in budding yeast.
Eriksson et al. (2012)
1 more

1 mention without citation

Structural and mechanistic insight into covalent substrate binding by Escherichia coli dihydroxyacetone kinase.
Shi et al. (2011)