2AK3

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

Replaces:  1AK3

Summary for 2AK3

• Entry DOI: 10.2210/pdb2ak3/pdb
• Descriptor: ADENYLATE KINASE ISOENZYME-3, SULFATE ION, ADENOSINE MONOPHOSPHATE, ... (4 entities in total)
• Functional Keywords: transferase (phosphotransferase)
• Biological source: Bos taurus (cattle)
• Cellular location: Mitochondrion matrix: P08760
• Total number of polymer chains: 2
• Total formula weight: 52037.10

Authors

Diederichs, K.,Schulz, G.E. (deposition date: 1995-03-07, release date: 1995-05-08, Last modification date: 2024-02-14)

Primary citation

Diederichs, K.,Schulz, G.E.
The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 A resolution.
J.Mol.Biol., 217:541-549, 1991

PubMed Abstract: The crystal structure of the complex between adenylate kinase from bovine mitochondrial matrix and its substrate AMP has been refined at 1.85 A resolution (1 A = 0.1 nm). Based on 42,519 independent reflections of better than 10 A resolution, a final R-factor of 18.9% was obtained with a model obeying standard geometry within 0.016 A in bond lengths and 3.2 degrees in bond angles. There are two enzyme: substrate complexes in the asymmetric unit, each consisting of 226 amino acid residues, one AMP and one sulfate ion. A superposition of the two full-length polypeptides revealed deviations that can be described as small relative movements of three domains. Best superpositions of individual domains yielded a residual overall root-mean-square deviation of 0.3 A for the backbone atoms and 0.5 A for the sidechains. The final model contains 381 solvent molecules in the asymmetric unit, 2 x 72 = 144 of which occupy corresponding positions in both complexes.

PubMed: 1994037
DOI: 10.1016/0022-2836(91)90756-V

Experimental method

X-RAY DIFFRACTION (1.85 Å)