› 2rh5

X-ray diffraction
2.48Å resolution

Structure of Apo Adenylate Kinase from Aquifex Aeolicus

Released:
DOI: 10.2210/pdb2rh5/pdb
PDB entry 2rh5 coloured by chain, front view.
PDB entry 2rh5 coloured by chain, side view.
PDB entry 2rh5 coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
Intrinsic motions along an enzymatic reaction trajectory.
Henzler-Wildman KA, Thai V, Lei M, Ott M, Wolf-Watz M, Fenn T, Pozharski E, Wilson MA, Petsko GA, Karplus M, Hübner CG, Kern D
Nature 450 838-44 (2007)
PMID: 18026086

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-130315 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylate kinase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 206 amino acids
Theoretical weight: 23.27 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O66490 (Residues: 1-206; Coverage: 100%)
Gene names: adk, aq_078
Sequence domains: Adenylate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2221
Unit cell:
a: 106.681Å b: 157.596Å c: 84.707Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.197 0.255
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

85 review citations

Dynamic personalities of proteins.
Henzler-Wildman et al. (2007)
84 more

16 mentions without citation

Conformational heterogeneity within the LID domain mediates substrate binding to Escherichia coli adenylate kinase: function follows fluctuations.
Schrank et al. (2013)
15 more