6BRA
HIV-1 protease (D25N, inactive) in complex with phage display optimized substrate SGIFLETS
Summary for 6BRA
| Entry DOI | 10.2210/pdb6bra/pdb |
| Descriptor | Protease, Phage display-optimized HIV-1 protease substrate, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | hiv, hiv-1, substrate, complex, phage display, recongition, hydrogen bonding, viral protein |
| Biological source | Human immunodeficiency virus 1 More |
| Total number of polymer chains | 3 |
| Total formula weight | 22474.12 |
| Authors | Windsor, I.W.,Raines, R.T. (deposition date: 2017-11-30, release date: 2018-07-18, Last modification date: 2023-10-04) |
| Primary citation | Windsor, I.W.,Raines, R.T. A substrate selected by phage display exhibits enhanced side-chain hydrogen bonding to HIV-1 protease. Acta Crystallogr D Struct Biol, 74:690-694, 2018 Cited by PubMed Abstract: Crystal structures of inactive variants of HIV-1 protease bound to peptides have revealed how the enzyme recognizes its endogenous substrates. The best of the known substrates is, however, a nonnatural substrate that was identified by directed evolution. The crystal structure of the complex between this substrate and the D25N variant of the protease is reported at a resolution of 1.1 Å. The structure has several unprecedented features, especially the formation of additional hydrogen bonds between the enzyme and the substrate. This work expands the understanding of molecular recognition by HIV-1 protease and informs the design of new substrates and inhibitors. PubMed: 29968678DOI: 10.1107/S2059798318006691 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.111 Å) |
Structure validation
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