1CA2

REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION

「1CAC」から置き換えられました

1CA2 の概要

• エントリーDOI: 10.2210/pdb1ca2/pdb
• 分子名称: CARBONIC ANHYDRASE II, ZINC ION (3 entities in total)
• 機能のキーワード: lyase(oxo-acid)
• 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: 29223.27

構造登録者

Eriksson, A.E.,Jones, T.A.,Liljas, A. (登録日: 1989-02-06, 公開日: 1990-01-15, 最終更新日: 2024-02-07)

主引用文献

Eriksson, A.E.,Jones, T.A.,Liljas, A.
Refined structure of human carbonic anhydrase II at 2.0 A resolution.
Proteins, 4:274-282, 1988

PubMed Abstract: The structure of human erythrocytic carbonic anhydrase II has been refined by constrained and restrained structure-factor least-squares refinement at 2.0 A resolution. The conventional crystallographic R value is 17.3%. Of 167 solvent molecules associated with the protein, four are buried and stabilize secondary structure elements. The zinc ion is ligated to three histidyl residues and one water molecule in a nearly tetrahedral geometry. In addition to the zinc-bound water, seven more water molecules are identified in the active site. Assuming that Glu-106 is deprotonated at pH 8.5, some of the hydrogen bond donor-acceptor relations in the active site can be assigned and are described here in detail. The O gamma 1 atom of Thr-199 donates its proton to the O epsilon 1 atom of Glu-106 and can function as a hydrogen bond acceptor only in additional hydrogen bonds.

PubMed: 3151019
DOI: 10.1002/prot.340040406

実験手法

X-RAY DIFFRACTION (2 Å)