› 3hpq

X-ray diffraction
2Å resolution

Crystal structure of wild-type adenylate kinase from E. coli, in complex with Ap5A

Released:
DOI: 10.2210/pdb3hpq/pdb
PDB entry 3hpq coloured by chain, front view.
PDB entry 3hpq coloured by chain, side view.
PDB entry 3hpq coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins.
Schrank TP, Bolen DW, Hilser VJ
Proc Natl Acad Sci U S A 106 16984-9 (2009)
PMID: 19805185

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159587 (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 K-12
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

1 bound ligand:
Ligand AP5 2 x AP5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P21212
Unit cell:
a: 83.646Å b: 72.639Å c: 78.699Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.199 0.245
Expression system: Escherichia coli

Quick links

Citations

15 review citations

The ensemble nature of allostery.
Motlagh et al. (2014)
14 more

5 mentions without citation

The role of protein conformational fluctuations in allostery, function, and evolution.
Wrabl et al. (2011)
4 more