2WHH

HIV-1 protease tethered dimer Q-product complex along with nucleophilic water molecule

2WHH の概要

• エントリーDOI: 10.2210/pdb2whh/pdb
• 分子名称: POL PROTEIN, PARA-NITROPHENYLALANINE, GLUTAMIC ACID, ... (4 entities in total)
• 機能のキーワード: protease, hydrolase, drug design, transferase, nucleotidyltransferase, rna-directed dna polymerase, catalytic mechanism, multifunctional enzyme, transition state, aspartyl protease
• 由来する生物種: HUMAN IMMUNODEFICIENCY VIRUS 1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22617.39

構造登録者

Prashar, V.,Bihani, S.,Das, A.,Ferrer, J.L.,Hosur, M.V. (登録日: 2009-05-05, 公開日: 2009-12-01, 最終更新日: 2023-12-13)

主引用文献

Prashar, V.,Bihani, S.,Das, A.,Ferrer, J.L.,Hosur, M.V.
Catalytic Water Co-Existing with a Product Peptide in the Active Site of HIV-1 Protease Revealed by X- Ray Structure Analysis.
Plos One, 4:E7860-, 2009

PubMed Abstract: It is known that HIV-1 protease is an important target for design of antiviral compounds in the treatment of Acquired Immuno Deficiency Syndrome (AIDS). In this context, understanding the catalytic mechanism of the enzyme is of crucial importance as transition state structure directs inhibitor design. Most mechanistic proposals invoke nucleophilic attack on the scissile peptide bond by a water molecule. But such a water molecule coexisting with any ligand in the active site has not been found so far in the crystal structures.

PubMed: 19924250
DOI: 10.1371/JOURNAL.PONE.0007860

実験手法

X-RAY DIFFRACTION (1.69 Å)