› 4ake

X-ray diffraction
2.2Å resolution

ADENYLATE KINASE

Released:
DOI: 10.2210/pdb4ake/pdb
PDB entry 4ake coloured by chain, front view.
PDB entry 4ake coloured by chain, side view.
PDB entry 4ake coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding.
Müller CW, Schlauderer GJ, Reinstein J, Schulz GE
Structure 4 147-56 (1996)
PMID: 8805521

Function and Biology Details

Reaction catalysed: 
ATP + AMP = 2 ADP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159588 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylate kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 214 amino acids
Theoretical weight: 23.62 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P69441 (Residues: 1-214; Coverage: 100%)
Gene names: JW0463, adk, b0474, dnaW, plsA
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 31.8Å b: 54.5Å c: 71.3Å
α: 67.7° β: 77.9° γ: 88.4°
R-values:
R R work R free
0.183 0.183 not available
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Molecular mechanisms of resistance to imatinib in Philadelphia-chromosome-positive leukaemias.
Gambacorti-Passerini et al. (2003)
7 more

161 mentions without citation

Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation.
Bahar et al. (2007)
160 more