1QJ4

HYDROXYNITRILE-LYASE FROM HEVEA BRASILIENSIS AT ATOMIC RESOLUTION

1QJ4 の概要

• エントリーDOI: 10.2210/pdb1qj4/pdb
• 関連するPDBエントリー: 1YAS
• 分子名称: HYDROXYNITRILE LYASE, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: oxynitrilase, cyanogenesis, cyanhydrin formation, lyase
• 由来する生物種: HEVEA BRASILIENSIS (PARA RUBBER TREE)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29738.94

構造登録者

Gugganig, M.,Gruber, K.,Kratky, C. (登録日: 1999-06-21, 公開日: 1999-10-10, 最終更新日: 2023-12-13)

主引用文献

Gruber, K.,Gugganig, M.,Wagner, U.G.,Kratky, C.
Atomic Resolution Crystal Structure of Hydroxynitrile Lyase from Hevea Brasiliensis
Biol.Chem., 380:993-, 1999

PubMed Abstract: The X-ray crystal structure of native hydroxynitrile lyase from Hevea brasiliensis (Hb-HNL) has been determined at 1.1 A resolution. It refined to a final R of 11.5% for all data and an Rfree of 14.4%. The favorable data-to-parameter ratio at atomic resolution made the refinement of individual anisotropic displacement parameters possible. The data also allowed a clear distinction of the alternate orientations of all histidine and the majority of asparagine and glutamine side chains. A number of hydrogen atoms, including one on the imidazole of the mechanistically important His-235, became visible as peaks in a difference electron density map. The structure revealed a discretely disordered sidechain of Ser-80, which is part of the putative catalytic triad. Analysis of the anisotropy indicated an increased mobility of residues near the entrance to the active site and within the active site.

PubMed: 10494852
DOI: 10.1515/BC.1999.123

実験手法

X-RAY DIFFRACTION (1.1 Å)