› 1ak2

X-ray diffraction
1.92Å resolution

ADENYLATE KINASE ISOENZYME-2

Released:
DOI: 10.2210/pdb1ak2/pdb
PDB entry 1ak2 coloured by chain, front view.
PDB entry 1ak2 coloured by chain, side view.
PDB entry 1ak2 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
The structure of bovine mitochondrial adenylate kinase: comparison with isoenzymes in other compartments.
Schlauderer GJ, Schulz GE
Protein Sci 5 434-41 (1996)
PMID: 8868479

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139947 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylate kinase 2, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 233 amino acids
Theoretical weight: 25.54 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P08166 (Residues: 2-233; Coverage: 96%)
Gene name: AK2
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 44.2Å b: 50.1Å c: 122.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.222 not available

Quick links

Citations

2 review citations

Dipeptidyl peptidase 9 substrates and their discovery: current progress and the application of mass spectrometry-based approaches.
Wilson et al. (2016)
1 more

15 mentions without citation

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