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1IGS

INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS AT 2.0 A RESOLUTION

1IGS の概要
エントリーDOI10.2210/pdb1igs/pdb
関連するPDBエントリー1A53 1LBF 1LBL
分子名称INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE, PHOSPHATE ION (3 entities in total)
機能のキーワードthermostable, tim-barrel, synthase
由来する生物種Sulfolobus solfataricus
タンパク質・核酸の鎖数1
化学式量合計28721.07
構造登録者
Hennig, M.,Darimont, B.,Kirschner, K.,Jansonius, J.N. (登録日: 1995-08-11, 公開日: 1996-07-11, 最終更新日: 2024-02-07)
主引用文献Hennig, M.,Darimont, B.,Sterner, R.,Kirschner, K.,Jansonius, J.N.
2.0 A structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability.
Structure, 3:1295-1306, 1995
Cited by
PubMed Abstract: Recent efforts to understand the basis of protein stability have focused attention on comparative studies of proteins from hyperthermophilic and mesophilic organisms. Most work to date has been on either oligomeric enzymes or monomers comprising more than one domain. Such studies are hampered by the need to distinguish between stabilizing interactions acting between subunits or domains from those acting within domains. In order to simplify the search for determinants of protein stability we have chosen to study the monomeric enzyme indole-3-glycerol phosphate synthase from the hyperthermophilic archaeon Sulfolobus solfataricus (sIGPS), which grows optimally at 90 degrees C.
PubMed: 8747456
DOI: 10.1016/S0969-2126(01)00267-2
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 1igs
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2024-10-30に公開中

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