2AK3

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

「1AK3」から置き換えられました

2AK3 の概要

• エントリーDOI: 10.2210/pdb2ak3/pdb
• 分子名称: ADENYLATE KINASE ISOENZYME-3, SULFATE ION, ADENOSINE MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: transferase (phosphotransferase)
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Mitochondrion matrix: P08760
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52037.10

構造登録者

Diederichs, K.,Schulz, G.E. (登録日: 1995-03-07, 公開日: 1995-05-08, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.85 Å)