- PDB-1gi5: 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: 1gi5
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. / Trypsin-like serine protease / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain / Trypsin ...: / 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. / Trypsin-like serine protease / Serine proteases, trypsin family, serine active site. / 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: 1.46→1.69 Å / Rmerge(I) obs: 0.261 / Num. unique all: 6275 / % possible all: 36.8
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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: 1.6→7 Å / σ(F): 1.8 / 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, Leu66, Ser86, Lys87, Ser110, Ser113, Ser130, Lys159, Ser166 Ser170, Ser217, Lys230, Ser236, Ser244 Note that HOH383 ...詳細: Residues simultaneously refined in two or more conformations are: Val53, Leu66, Ser86, Lys87, Ser110, Ser113, Ser130, Lys159, Ser166 Ser170, Ser217, Lys230, Ser236, Ser244 Note that HOH383 makes short H-bonds to OgSer195 and O6' of the inhibitor Disordered waters are: HOH600 which is close to HOH601, which in turn is close to HOH602; HOH465 which is close to sulfate_466; HOH396 which is close to HOH397; HOH422 which is close to a symmetry-related equivelent of HOH423 HOH654 which occupies the space available when Lys87 is in conformation # 1. HOH674 which is close to HOH675; HOH696 which is close to HOH697; His40 and HIS91 are MONOPROTONATED ON THE EPSILON NITROGEN. His57 is doubly protonatd.