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1CZI

CHYMOSIN COMPLEX WITH THE INHIBITOR CP-113972

1CZI の概要
エントリーDOI10.2210/pdb1czi/pdb
関連するBIRD辞書のPRD_IDPRD_000344
分子名称CHYMOSIN, CP-113972 (NORSTATINE-S-METHYL CYSTEINE-IODO-PHENYLALANINE-PROLINE) (3 entities in total)
機能のキーワードacid proteinase, aspartyl protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
由来する生物種Bos taurus (cattle)
タンパク質・核酸の鎖数2
化学式量合計36403.39
構造登録者
Groves, M.R.,Dhanaraj, V.,Pitts, J.E.,Badasso, M.,Hoover, D.,Nugent, P.,Blundell, T.L. (登録日: 1997-01-15, 公開日: 1997-04-01, 最終更新日: 2023-11-15)
主引用文献Groves, M.R.,Dhanaraj, V.,Badasso, M.,Nugent, P.,Pitts, J.E.,Hoover, D.J.,Blundell, T.L.
A 2.3 A resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site beta-hairpin flap is rearranged when compared with the native crystal structure.
Protein Eng., 11:833-840, 1998
Cited by
PubMed Abstract: In the crystal structure of uncomplexed native chymosin, the beta-hairpin at the active site, known as 'the flap', adopts a different conformation from that of other aspartic proteinases. This conformation would prevent the mode of binding of substrates/inhibitors generally found in other aspartic proteinase complexes. We now report the X-ray analysis of chymosin complexed with a reduced bond inhibitor CP-113972 ¿(2R,3S)-isopropyl 3-[(L-prolyl-p-iodo-L-phenylalanyl-S-methyl-cysteinyl)amino-4]-cyclohexy l-2-hydroxybutanoate¿ at 2.3 A resolution in a novel crystal form of spacegroup R32. The structure has been refined by restrained least-squares methods to a final R-factor of 0.19 for a total of 11 988 independent reflections in the resolution range 10 to 2.3 A. The extended beta-strand conformation of the inhibitor allows hydrogen bonds within the active site, while its sidechains make both electrostatic and hydrophobic interactions with residues lining the specificity pockets S4-->S1. The flap closes over the active site cleft in a way that closely resembles that of other previously determined aspartic proteinase inhibitor complexes. We conclude that the usual position and conformation of the flap found in other aspartic proteinases is available to native chymosin. The conformation observed in the native crystal form may result from intermolecular interactions between symmetry-related molecules in the crystal lattice.
PubMed: 9862200
DOI: 10.1093/protein/11.10.833
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.3 Å)
構造検証レポート
Validation report summary of 1czi
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2025-07-09に公開中

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