› 2ak3

X-ray diffraction
1.85Å resolution

THE THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN MITOCHONDRIAL MATRIX ADENYLATE KINASE AND ITS SUBSTRATE AMP AT 1.85 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb2ak3/pdb
PDB entry 2ak3 coloured by chain, front view.
PDB entry 2ak3 coloured by chain, side view.
PDB entry 2ak3 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 A resolution.
Diederichs K, Schulz GE
J Mol Biol 217 541-9 (1991)
PMID: 1994037

Function and Biology Details

Reaction catalysed: 
NTP + AMP = NDP + 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-140374 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTP:AMP phosphotransferase AK3, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 226 amino acids
Theoretical weight: 25.58 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P08760 (Residues: 2-227; Coverage: 100%)
Gene names: AK3, AK3L1
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand AMP 2 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 49.83Å b: 66.99Å c: 155.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Not provided

Quick links

Citations

3 review citations

Fold change in evolution of protein structures.
Grishin NV. (2001)
2 more

25 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
24 more