4Z50
Crystal Structure of Multidrug Resistant HIV-1 Protease Clinical Isolate PR20D25N with Tucked Flap
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0055036 | cellular_component | virion membrane |
| A | 0072494 | cellular_component | host multivesicular body |
| B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0055036 | cellular_component | virion membrane |
| B | 0072494 | cellular_component | host multivesicular body |
| C | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008233 | molecular_function | peptidase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0055036 | cellular_component | virion membrane |
| C | 0072494 | cellular_component | host multivesicular body |
| D | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008233 | molecular_function | peptidase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0055036 | cellular_component | virion membrane |
| D | 0072494 | cellular_component | host multivesicular body |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 101 |
| Chain | Residue |
| A | GLU21 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 201 |
| Chain | Residue |
| B | LYS155 |
| D | TRP106 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 202 |
| Chain | Residue |
| B | GLU121 |
| B | HOH378 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 203 |
| Chain | Residue |
| B | LYS107 |
| B | ARG108 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 204 |
| Chain | Residue |
| B | HOH306 |
| B | HOH349 |
| B | HOH363 |
| B | HOH386 |
| B | ASP160 |
| B | HOH305 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue NA B 205 |
| Chain | Residue |
| B | LEU119 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 206 |
| Chain | Residue |
| B | THR112 |
| B | GLU165 |
| B | ALA167 |
| B | GLY168 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 101 |
| Chain | Residue |
| C | LYS7 |
| C | ARG8 |
| C | HOH227 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 102 |
| Chain | Residue |
| C | GLU21 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 103 |
| Chain | Residue |
| C | ARG8 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue NA C 104 |
| Chain | Residue |
| C | ASP60 |
| C | HOH218 |
| C | HOH243 |
| C | HOH255 |
| C | HOH265 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue CL D 201 |
| Chain | Residue |
| D | GLU121 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 202 |
| Chain | Residue |
| D | LYS107 |
| D | ARG108 |
| D | HOH366 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue NA D 203 |
| Chain | Residue |
| D | ASP160 |
| D | HOH302 |
| D | HOH324 |
| D | HOH349 |
| D | HOH364 |
| D | HOH380 |
| D | HOH390 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 204 |
| Chain | Residue |
| A | HOH270 |
| D | HIS169 |
| D | GLN192 |
| D | ILE193 |
| D | HOH308 |
| D | HOH326 |
