1CYO

BOVINE CYTOCHROME B(5)

「3B5C」から置き換えられました 「1B5C」から置き換えられました 「2B5C」から置き換えられました

1CYO の概要

• エントリーDOI: 10.2210/pdb1cyo/pdb
• 分子名称: CYTOCHROME B5, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: electron transport
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side: P00171
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11268.21

構造登録者

Durley, R.C.E.,Mathews, F.S. (登録日: 1994-08-03, 公開日: 1994-11-30, 最終更新日: 2024-02-07)

主引用文献

Durley, R.C.,Mathews, F.S.
Refinement and structural analysis of bovine cytochrome b5 at 1.5 A resolution.
Acta Crystallogr.,Sect.D, 52:65-76, 1996

PubMed Abstract: The structure of bovine liver cytochrome b(5), a soluble 93-residue proteolytic fragment of a 16 kDa membrane-bound hemoprotein, initially solved at 2.0 A resolution, has been refined at 1.5 A using data collected on a diffractometer. Refinement to 2.0 A resolution used the Hendrickson-Konnert procedure PROLSQ and was then extended to 1.5 A resolution using the program PROFFT. Only residues 3-87 could be identified in the model and these residues together with 93 water molecules gave an agreement factor of R = 0.161 for data in the resolution range 1.5-5 A. The structure was finally refined using the program X-PLOR, which enabled alternate conformers to be modelled for several surface side chains. Residues 1 and 2 at the amino terminus of the protein and residue 88 near the carboxyl terminus could be identified from these electron-density maps. However the remaining disordered carboxy-terminal residues could not successfully be included in the model. A total of 117 solvent molecules were included in the final refinement to give R = 0.164 for the data between 1.5 and 10 A.

PubMed: 15299727
DOI: 10.1107/S0907444995007827

実験手法

X-RAY DIFFRACTION (1.5 Å)