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2FTN

E. coli thymidylate synthase Y94F mutant

2FTN の概要
エントリーDOI10.2210/pdb2ftn/pdb
関連するPDBエントリー2fto 2ftq
分子名称Thymidylate synthase, SULFATE ION (3 entities in total)
機能のキーワードmethyltransferase, transferase
由来する生物種Escherichia coli
細胞内の位置Cytoplasm: P0A884
タンパク質・核酸の鎖数1
化学式量合計31312.17
構造登録者
Montfort, W.R.,Roberts, S.A. (登録日: 2006-01-24, 公開日: 2006-05-02, 最終更新日: 2024-10-30)
主引用文献Roberts, S.A.,Hyatt, D.C.,Honts, J.E.,Changchien, L.,Maley, G.F.,Maley, F.,Montfort, W.R.
Structure of the Y94F mutant of Escherichia coli thymidylate synthase.
ACTA CRYSTALLOGR.,SECT.F, 62:840-843, 2006
Cited by
PubMed Abstract: Tyr94 of Escherichia coli thymidylate synthase is thought to be involved, either directly or by activation of a water molecule, in the abstraction of a proton from C5 of the 2'-deoxyuridine 5'-monophosphate (dUMP) substrate. Mutation of Tyr94 leads to a 400-fold loss in catalytic activity. The structure of the Y94F mutant has been determined in the native state and as a ternary complex with thymidine 5'-monophosphate (dTMP) and 10-propargyl 5,8-dideazafolate (PDDF). There are no structural changes ascribable to the mutation other than loss of a water molecule hydrogen bonded to the tyrosine OH, which is consistent with a catalytic role for the phenolic OH.
PubMed: 16946460
DOI: 10.1107/S1744309106029691
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.6 Å)
構造検証レポート
Validation report summary of 2ftn
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2026-04-01に公開中

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