1LUG

Full Matrix Error Analysis of Carbonic Anhydrase

1LUG の概要

• エントリーDOI: 10.2210/pdb1lug/pdb
• 関連するPDBエントリー: 3K34
• 分子名称: Carbonic Anhydrase II, ZINC ION, MERCURY (II) ION, ... (7 entities in total)
• 機能のキーワード: error analysis, full-matrix, metalloenzyme, lyase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P00918
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30272.21

構造登録者

Merritt, E.A.,Le Trong, I.,Behnke, C.A. (登録日: 2002-05-22, 公開日: 2003-09-09, 最終更新日: 2024-02-14)

主引用文献

Behnke, C.A.,Le Trong, I.,Godden, J.W.,Merritt, E.A.,Teller, D.C.,Bajorath, J.,Stenkamp, R.E.
Atomic resolution studies of carbonic anhydrase II.
Acta Crystallogr.,Sect.D, 66:616-627, 2010

PubMed Abstract: Carbonic anhydrase has been well studied structurally and functionally owing to its importance in respiration. A large number of X-ray crystallographic structures of carbonic anhydrase and its inhibitor complexes have been determined, some at atomic resolution. Structure determination of a sulfonamide-containing inhibitor complex has been carried out and the structure was refined at 0.9 A resolution with anisotropic atomic displacement parameters to an R value of 0.141. The structure is similar to those of other carbonic anhydrase complexes, with the inhibitor providing a fourth nonprotein ligand to the active-site zinc. Comparison of this structure with 13 other atomic resolution (higher than 1.25 A) isomorphous carbonic anhydrase structures provides a view of the structural similarity and variability in a series of crystal structures. At the center of the protein the structures superpose very well. The metal complexes superpose (with only two exceptions) with standard deviations of 0.01 A in some zinc-protein and zinc-ligand bond lengths. In contrast, regions of structural variability are found on the protein surface, possibly owing to flexibility and disorder in the individual structures, differences in the chemical and crystalline environments or the different approaches used by different investigators to model weak or complicated electron-density maps. These findings suggest that care must be taken in interpreting structural details on protein surfaces on the basis of individual X-ray structures, even if atomic resolution data are available.

PubMed: 20445237
DOI: 10.1107/S0907444910006554

実験手法

X-RAY DIFFRACTION (0.95 Å)