5TV3
Crystal structure of the complex of Helicobacter pylori alpha-carbonic anhydrase with (E)-5-(((4-(tert-butyl)phenyl)sulfonyl)imino)-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004089 | molecular_function | carbonate dehydratase activity |
| A | 0006885 | biological_process | regulation of pH |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0015670 | biological_process | carbon dioxide transport |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004089 | molecular_function | carbonate dehydratase activity |
| B | 0006885 | biological_process | regulation of pH |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0015670 | biological_process | carbon dioxide transport |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004089 | molecular_function | carbonate dehydratase activity |
| C | 0006885 | biological_process | regulation of pH |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0015670 | biological_process | carbon dioxide transport |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004089 | molecular_function | carbonate dehydratase activity |
| D | 0006885 | biological_process | regulation of pH |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0015670 | biological_process | carbon dioxide transport |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0004089 | molecular_function | carbonate dehydratase activity |
| E | 0006885 | biological_process | regulation of pH |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0015670 | biological_process | carbon dioxide transport |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0004089 | molecular_function | carbonate dehydratase activity |
| F | 0006885 | biological_process | regulation of pH |
| F | 0008270 | molecular_function | zinc ion binding |
| F | 0015670 | biological_process | carbon dioxide transport |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0004089 | molecular_function | carbonate dehydratase activity |
| G | 0006885 | biological_process | regulation of pH |
| G | 0008270 | molecular_function | zinc ion binding |
| G | 0015670 | biological_process | carbon dioxide transport |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0004089 | molecular_function | carbonate dehydratase activity |
| H | 0006885 | biological_process | regulation of pH |
| H | 0008270 | molecular_function | zinc ion binding |
| H | 0015670 | biological_process | carbon dioxide transport |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS110 |
| A | HIS112 |
| A | HIS129 |
| A | THR191 |
| A | 7L3302 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue 7L3 A 302 |
| Chain | Residue |
| A | HIS129 |
| A | LEU139 |
| A | LEU190 |
| A | THR191 |
| A | ALA192 |
| A | PRO193 |
| A | ZN301 |
| A | LYS88 |
| A | ASN108 |
| A | HIS110 |
| A | HIS112 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS110 |
| B | HIS112 |
| B | HIS129 |
| B | 7L3302 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue 7L3 B 302 |
| Chain | Residue |
| B | LYS88 |
| B | ASN108 |
| B | HIS110 |
| B | HIS112 |
| B | HIS129 |
| B | LYS133 |
| B | LEU139 |
| B | VAL141 |
| B | LEU190 |
| B | THR191 |
| B | ALA192 |
| B | PRO193 |
| B | TRP201 |
| B | ZN301 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue ZN C 301 |
| Chain | Residue |
| C | HIS110 |
| C | HIS112 |
| C | HIS129 |
| C | THR191 |
| C | 7L3303 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 302 |
| Chain | Residue |
| C | HIS84 |
| C | THR86 |
| C | LYS88 |
| C | HIS110 |
| C | ALA192 |
| C | 7L3303 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | binding site for residue 7L3 C 303 |
| Chain | Residue |
| C | LYS88 |
| C | ASP107 |
| C | ASN108 |
| C | HIS110 |
| C | HIS112 |
| C | HIS129 |
| C | LYS133 |
| C | VAL141 |
| C | LEU190 |
| C | THR191 |
| C | ALA192 |
| C | PRO193 |
| C | TRP201 |
| C | ZN301 |
| C | GOL302 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 301 |
| Chain | Residue |
| D | HIS110 |
| D | HIS112 |
| D | HIS129 |
| D | THR191 |
| D | 7L3303 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 302 |
| Chain | Residue |
| D | MET115 |
| D | GLU116 |
| D | PHE117 |
| D | SER127 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residue 7L3 D 303 |
| Chain | Residue |
| D | LYS88 |
| D | ASN108 |
| D | HIS110 |
| D | HIS112 |
| D | HIS129 |
| D | LYS133 |
| D | VAL141 |
| D | LEU190 |
| D | THR191 |
| D | ALA192 |
| D | PRO193 |
| D | ZN301 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN E 301 |
| Chain | Residue |
| E | HIS110 |
| E | HIS112 |
| E | HIS129 |
| E | THR191 |
| E | 7L3302 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for residue 7L3 E 302 |
| Chain | Residue |
| E | LYS88 |
| E | ASN108 |
| E | HIS110 |
| E | HIS112 |
| E | HIS129 |
| E | VAL131 |
| E | VAL141 |
| E | LEU190 |
| E | THR191 |
| E | ALA192 |
| E | PRO193 |
| E | ZN301 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue ZN F 301 |
| Chain | Residue |
| F | HIS112 |
| F | GLU116 |
| F | HIS129 |
| F | THR191 |
| F | 7L3302 |
| F | HIS110 |
| site_id | AD5 |
| Number of Residues | 13 |
| Details | binding site for residue 7L3 F 302 |
| Chain | Residue |
| F | LYS88 |
| F | ASN108 |
| F | HIS110 |
| F | HIS112 |
| F | HIS129 |
| F | VAL131 |
| F | LYS133 |
| F | LEU139 |
| F | VAL141 |
| F | LEU190 |
| F | THR191 |
| F | ALA192 |
| F | ZN301 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue ZN G 301 |
| Chain | Residue |
| G | HIS110 |
| G | HIS112 |
| G | HIS129 |
| G | THR191 |
| G | 7L3303 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue CL G 302 |
| Chain | Residue |
| G | MET115 |
| G | GLU116 |
| G | PHE117 |
| G | SER127 |
| G | HIS129 |
| site_id | AD8 |
| Number of Residues | 14 |
| Details | binding site for residue 7L3 G 303 |
| Chain | Residue |
| G | ASP107 |
| G | ASN108 |
| G | HIS110 |
| G | HIS112 |
| G | HIS129 |
| G | LYS133 |
| G | GLY137 |
| G | VAL141 |
| G | LEU190 |
| G | THR191 |
| G | ALA192 |
| G | PRO193 |
| G | TRP201 |
| G | ZN301 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN H 301 |
| Chain | Residue |
| H | HIS110 |
| H | HIS112 |
| H | HIS129 |
| H | 7L3302 |
| site_id | AE1 |
| Number of Residues | 14 |
| Details | binding site for residue 7L3 H 302 |
| Chain | Residue |
| H | LYS88 |
| H | ASP107 |
| H | ASN108 |
| H | HIS110 |
| H | HIS112 |
| H | HIS129 |
| H | VAL131 |
| H | LYS133 |
| H | VAL141 |
| H | LEU190 |
| H | THR191 |
| H | ALA192 |
| H | PRO193 |
| H | ZN301 |
