- PDB-1gi1: 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: 1gi1
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: 1.42→1.48 Å / Rmerge(I) obs: 0.25 / Num. unique all: 1822 / % possible all: 35.7
反射
*PLUS
Num. measured all: 72876
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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: 1.42→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: Thr26, Val31, Ser49, Gln50, Val53, Leu67, Met104, Ser110, Ser116, Lys224, Ser236. Note that HOH383 makes short H-bonds to ...詳細: Residues simultaneously refined in two or more conformations are: Thr26, Val31, Ser49, Gln50, Val53, Leu67, Met104, Ser110, Ser116, Lys224, Ser236. Note that HOH383 makes short H-bonds to OgSer195 and O6' of the inhibitor Disordered waters are: HOH335 which is close to HOH336; HOH345 which is close to HOH346; HOH381 which is close to HOH382; HOH417 which is close to HOH418; HOH431 which is close to HOH432; HOH509 which is close to HOH510; HOH511 which is close to HOH512; HOH513 which is close to HOH514; HOH513 which is close to a symmetry-related equivalent of HOH528; HOH535 which is close to HOH536; HIS91 is MONOPROTONATED ON THE EPSILON NITROGEN. His57 is doubly protonatd.