- PDB-1gi2: A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTER... -
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基本情報
登録情報
データベース: PDB / ID: 1gi2
タイトル
A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE
要素
BETA-TRYPSIN
キーワード
HYDROLASE / three-centered / very short hydrogen bond / oxyanion hole water / shift of pKa of His57 / structure-based drug design / specificity / urokinase / trypsin / thrombin / Zn+2-mediated inhibition
機能・相同性
機能・相同性情報
trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding 類似検索 - 分子機能
Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases ...Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases / Thrombin, subunit H / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta 類似検索 - ドメイン・相同性
解像度: 1.38→1.44 Å / Rmerge(I) obs: 0.275 / Num. unique all: 1889 / % possible all: 34.1
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解析
ソフトウェア
名称
バージョン
分類
bioteX
データ収集
bioteX
データ削減
X-PLOR
3.851
精密化
bioteX
データスケーリング
精密化
構造決定の手法: フーリエ合成 / 解像度: 1.38→7 Å / σ(F): 1.7 / 立体化学のターゲット値: X-PLOR force field 詳細: Residues simultaneously refined in two or more conformations are: Val53, Ser61, Ser84, Ser86, Leu99, Met104, Ser113, Ser116, Arg117, Ser127 Gln135, Ser146, Asp165, Ser166, Ser167, Gln175, ...詳細: Residues simultaneously refined in two or more conformations are: Val53, Ser61, Ser84, Ser86, Leu99, Met104, Ser113, Ser116, Arg117, Ser127 Gln135, Ser146, Asp165, Ser166, Ser167, Gln175, Ser217, Ser236, Ser244. Note that HOH383 makes short H-bonds to OgSer195 and O6' of the inhibitor Disordered waters are: HOH379 which is close to sulfate_380; HOH425 which is close to HOH426; HOH461 which is close to a symmetry-related equivalent of HOH462; HOH604 which is close to HOH605; HIS91 is MONOPROTONATED ON THE EPSILON NITROGEN. His57 is doubly protonatd.