1F28

CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII BOUND TO DUMP AND BW1843U89

1F28 の概要

• エントリーDOI: 10.2210/pdb1f28/pdb
• 関連するPDBエントリー: 1CI7
• 分子名称: THYMIDYLATE SYNTHASE, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, S)-2-(5(((1,2-DIHYDRO-3-METHYL-1-OXOBENZO(F)QUINAZOLIN-9-YL)METHYL)AMINO)1-OXO-2-ISOINDOLINYL)GLUTARIC ACID, ... (4 entities in total)
• 機能のキーワード: beta-sheet, protein-inhibitor complex, transferase
• 由来する生物種: Pneumocystis carinii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 140847.86

構造登録者

Anderson, A.C.,O'Neil, R.H.,Surti, T.S.,Stroud, R.M. (登録日: 2000-05-23, 公開日: 2001-06-06, 最終更新日: 2024-11-13)

主引用文献

Anderson, A.C.,O'Neil, R.H.,Surti, T.S.,Stroud, R.M.
Approaches to solving the rigid receptor problem by identifying a minimal set of flexible residues during ligand docking.
Chem.Biol., 8:445-457, 2001

PubMed Abstract: Using fixed receptor sites derived from high-resolution crystal structures in structure-based drug design does not properly account for ligand-induced enzyme conformational change and imparts a bias into the discovery and design of novel ligands. We sought to facilitate the design of improved drug leads by defining residues most likely to change conformation, and then defining a minimal manifold of possible conformations of a target site for drug design based on a small number of identified flexible residues.

PubMed: 11358692
DOI: 10.1016/S1074-5521(01)00023-0

実験手法

X-RAY DIFFRACTION (1.9 Å)