2WHH
HIV-1 protease tethered dimer Q-product complex along with nucleophilic water molecule
Summary for 2WHH
| Entry DOI | 10.2210/pdb2whh/pdb |
| Descriptor | POL PROTEIN, PARA-NITROPHENYLALANINE, GLUTAMIC ACID, ... (4 entities in total) |
| Functional Keywords | protease, hydrolase, drug design, transferase, nucleotidyltransferase, rna-directed dna polymerase, catalytic mechanism, multifunctional enzyme, transition state, aspartyl protease |
| Biological source | HUMAN IMMUNODEFICIENCY VIRUS 1 |
| Total number of polymer chains | 1 |
| Total formula weight | 22617.39 |
| Authors | Prashar, V.,Bihani, S.,Das, A.,Ferrer, J.L.,Hosur, M.V. (deposition date: 2009-05-05, release date: 2009-12-01, Last modification date: 2023-12-13) |
| Primary citation | 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 Cited by 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: 19924250DOI: 10.1371/JOURNAL.PONE.0007860 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.69 Å) |
Structure validation
Download full validation report
