2HMQ

THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION

「1HMQ」から置き換えられました 「1HMM」から置き換えられました 「1HMN」から置き換えられました

2HMQ の概要

• エントリーDOI: 10.2210/pdb2hmq/pdb
• 分子名称: HEMERYTHRIN, ACETATE ION, MU-OXO-DIIRON, ... (4 entities in total)
• 機能のキーワード: oxygen transport
• 由来する生物種: Themiste dyscritum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 54158.92

構造登録者

Holmes, M.A.,Stenkamp, R.E. (登録日: 1990-10-18, 公開日: 1992-01-15, 最終更新日: 2024-06-05)

主引用文献

Holmes, M.A.,Stenkamp, R.E.
Structures of met and azidomet hemerythrin at 1.66 A resolution.
J.Mol.Biol., 220:723-737, 1991

PubMed Abstract: The crystallographic refinement of met and azidomet hemerythrin has been carried out at 1.66 A resolution in an attempt to characterize precisely the binuclear iron center in this protein. Restrained least-squares refinement has produced molecular models giving R-values of 18.9% for met (65,683 reflections from 10 A to 1.66 A) and 17.6% for azidomet hemerythrin (68,747 reflections from 10.0 A to 1.66 A). The protein structure in each derivative is very similar to that of myohemerythrin. The mu-oxo bridged iron center differs between the two forms. The complex in met hemerythrin is asymmetric with the bridging oxygen closer to one of the iron atoms while the complex in azidomet hemerythrin is symmetric. After investigations of the effects of correlation in the refinement, we believe this difference between the two complexes is associated with chemical differences and is not a refinement artefact.

PubMed: 1870128
DOI: 10.1016/0022-2836(91)90113-K

実験手法

X-RAY DIFFRACTION (1.66 Å)