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2PCY

THE CRYSTAL STRUCTURE OF POPLAR APOPLASTOCYANIN AT 1.8-ANGSTROMS RESOLUTION. THE GEOMETRY OF THE COPPER-BINDING SITE IS CREATED BY THE POLYPEPTIDE

2PCY の概要
エントリーDOI10.2210/pdb2pcy/pdb
分子名称PLASTOCYANIN (2 entities in total)
機能のキーワードelectron transport protein(cuproprotein)
由来する生物種Populus nigra
細胞内の位置Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:1492962, ECO:0000269|PubMed:22883960, ECO:0000269|PubMed:6620385, ECO:0000269|PubMed:6698995, ECO:0000269|Ref: P00299
タンパク質・核酸の鎖数1
化学式量合計10493.61
構造登録者
Garrett, T.P.J.,Guss, J.M.,Freeman, H.C. (登録日: 1983-11-03, 公開日: 1984-02-02, 最終更新日: 2024-02-21)
主引用文献Garrett, T.P.,Clingeleffer, D.J.,Guss, J.M.,Rogers, S.J.,Freeman, H.C.
The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide
J.Biol.Chem., 259:2822-2825, 1984
Cited by
PubMed Abstract: The three-dimensional structure of apoplastocyanin from poplar leaves (Populus nigra var. italica) has been determined by x-ray diffraction at 1.8-A resolution. The structure closely resembles that of the holoprotein. In particular, the positions of the copper-binding residues in the apo- and holoproteins differ by only 0.1-0.3 A. This indicates that the irregular geometry of the "type 1" copper site is imposed upon the metal atom by the polypeptide moiety. A 180 degrees rotation of one solvent-exposed histidine imidazole ring about C beta-C gamma appears to facilitate access to the copper site. The close structural similarity between apo-, Cu-(II)-, and Cu(I)-plastocyanin was initially demonstrated by means of electron density difference maps. Two series of restrained least squares refinement calculations for apoplastocyanin, originating from different sets of atomic positional parameters, were carried out in parallel. Both refinements converged to the same model which, when fully refined, had a residual R = 0.16. Forty-two water molecules were located during the refinement.
PubMed: 6698995
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.8 Å)
構造検証レポート
Validation report summary of 2pcy
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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