1U8G
Crystal structure of a HIV-1 Protease in complex with peptidomimetic inhibitor KI2-PHE-GLU-GLU-NH2
Summary for 1U8G
| Entry DOI | 10.2210/pdb1u8g/pdb |
| Related | 1NH0 |
| Related PRD ID | PRD_000401 |
| Descriptor | PROTEASE RETROPEPSIN, peptidomimetic inhibitor KI2-PHE-GLU-GLU-NH2 (3 entities in total) |
| Functional Keywords | aspartyl protease, human immunodeficiency virus, inhibitor design, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Human immunodeficiency virus 1 |
| Cellular location | Gag-Pol polyprotein: Host cell membrane ; Lipid-anchor. Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P03367 |
| Total number of polymer chains | 3 |
| Total formula weight | 22340.27 |
| Authors | Brynda, J.,Rezacova, P.,Fabry, M.,Horejsi, M.,Hradilek, M.,Soucek, R.,Stouracova, R.,Konvalinka, J.,Sedlacek, J. (deposition date: 2004-08-06, release date: 2004-11-02, Last modification date: 2018-02-14) |
| Primary citation | Brynda, J.,Rezacova, P.,Fabry, M.,Horejsi, M.,Stouracova, R.,Soucek, M.,Hradilek, M.,Konvalinka, J.,Sedlacek, J. Inhibitor binding at the protein interface in crystals of a HIV-1 protease complex. Acta Crystallogr.,Sect.D, 60:1943-1948, 2004 Cited by PubMed Abstract: Depending on the excess of ligand used for complex formation, the HIV-1 protease complexed with a novel phenylnorstatine inhibitor forms crystals of either hexagonal (P6(1)) or orthorhombic (P2(1)2(1)2(1)) symmetry. The orthorhombic form shows an unusual complexity of crystal packing: in addition to one inhibitor molecule that is bound to the enzyme active site, the second inhibitor molecule is bound as an outer ligand at the protein interface. Binding of the outer ligand apparently increases the crystal-quality parameters so that the diffraction data allow solution of the structure of the complex at 1.03 A, the best resolution reported to date. The outer ligand interacts with all four surrounding HIV-1 protease molecules and has a bent conformation owing to its accommodation in the intermolecular space. The parameters of the solved structures of the orthorhombic and hexagonal forms are compared. PubMed: 15502300DOI: 10.1107/S0907444904021572 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.201 Å) |
Structure validation
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