2PQT

Human N-acetyltransferase 1

2PQT の概要

• エントリーDOI: 10.2210/pdb2pqt/pdb
• 分子名称: Arylamine N-acetyltransferase 1, CHLORIDE ION, UNKNOWN ATOM OR ION, ... (4 entities in total)
• 機能のキーワード: arylamine n-acetyltransferase 1, arylamide acetylase 1, structural genomics consortium, sgc, bromoacetanilide, covalent, inhibitor, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P18440
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34443.48

構造登録者

Tempel, W.,Wu, H.,Dombrovski, L.,Loppnau, P.,Weigelt, J.,Sundstrom, M.,Arrowsmith, C.H.,Edwards, A.M.,Grant, D.M.,Bochkarev, A.,Plotnikov, A.N.,Structural Genomics Consortium (SGC) (登録日: 2007-05-02, 公開日: 2007-05-15, 最終更新日: 2023-08-30)

主引用文献

Wu, H.,Dombrovsky, L.,Tempel, W.,Martin, F.,Loppnau, P.,Goodfellow, G.H.,Grant, D.M.,Plotnikov, A.N.
Structural Basis of Substrate-binding Specificity of Human Arylamine N-Acetyltransferases.
J.Biol.Chem., 282:30189-30197, 2007

PubMed Abstract: The human arylamine N-acetyltransferases NAT1 and NAT2 play an important role in the biotransformation of a plethora of aromatic amine and hydrazine drugs. They are also able to participate in the bioactivation of several known carcinogens. Each of these enzymes is genetically variable in human populations, and polymorphisms in NAT genes have been associated with various cancers. Here we have solved the high resolution crystal structures of human NAT1 and NAT2, including NAT1 in complex with the irreversible inhibitor 2-bromoacetanilide, a NAT1 active site mutant, and NAT2 in complex with CoA, and have refined them to 1.7-, 1.8-, and 1.9-A resolution, respectively. The crystal structures reveal novel structural features unique to human NATs and provide insights into the structural basis of the substrate specificity and genetic polymorphism of these enzymes.

PubMed: 17656365
DOI: 10.1074/jbc.M704138200

実験手法

X-RAY DIFFRACTION (1.78 Å)