3QU2
Crystal structure of pyrophosphatase from bacteroides thetaiotaomicron, a closed cap conformation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008801 | molecular_function | beta-phosphoglucomutase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050308 | molecular_function | sugar-phosphatase activity |
| B | 0008801 | molecular_function | beta-phosphoglucomutase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050308 | molecular_function | sugar-phosphatase activity |
| C | 0008801 | molecular_function | beta-phosphoglucomutase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050308 | molecular_function | sugar-phosphatase activity |
| D | 0008801 | molecular_function | beta-phosphoglucomutase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050308 | molecular_function | sugar-phosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 225 |
| Chain | Residue |
| A | ASP11 |
| A | ASP13 |
| A | GLU47 |
| A | ASN172 |
| A | HOH549 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 226 |
| Chain | Residue |
| A | HOH598 |
| D | LEU208 |
| A | ASN191 |
| A | GLY197 |
| A | PRO210 |
| A | HOH234 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 225 |
| Chain | Residue |
| B | ASP11 |
| B | ASP13 |
| B | GLU47 |
| B | ASN172 |
| B | HOH263 |
| B | HOH276 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 226 |
| Chain | Residue |
| B | ASP13 |
| B | TRP27 |
| B | GLY48 |
| B | ARG49 |
| B | CL228 |
| B | HOH263 |
| B | HOH284 |
| B | HOH487 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 227 |
| Chain | Residue |
| B | ASN191 |
| B | GLY197 |
| B | LEU208 |
| B | PRO210 |
| B | HOH255 |
| B | HOH600 |
| B | HOH736 |
| C | LEU208 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 225 |
| Chain | Residue |
| C | ASP11 |
| C | ASP13 |
| C | GLU47 |
| C | ASN172 |
| C | HOH568 |
| C | HOH569 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 225 |
| Chain | Residue |
| D | ASP11 |
| D | ASP13 |
| D | GLU47 |
| D | ASN172 |
| D | HOH272 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 226 |
| Chain | Residue |
| D | ASP13 |
| D | HIS23 |
| D | TRP27 |
| D | GLY48 |
| D | ARG49 |
| D | HOH241 |
| D | HOH272 |
| D | HOH410 |
| D | HOH603 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 227 |
| Chain | Residue |
| A | LEU208 |
| D | ASN191 |
| D | GLY197 |
| D | PRO210 |
| D | HOH257 |
| D | HOH269 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 228 |
| Chain | Residue |
| D | LEU121 |
| D | GLU125 |
| D | PHE132 |
| D | LYS134 |
| D | MET137 |
| D | HOH432 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 228 |
| Chain | Residue |
| B | ASP11 |
| B | GLY114 |
| B | LYS147 |
| B | GOL226 |
| B | HOH487 |
| site_id | BC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CIT A 227 |
| Chain | Residue |
| A | ASP13 |
| A | MET20 |
| A | HIS23 |
| A | TRP27 |
| A | GLU47 |
| A | GLY48 |
| A | ARG49 |
| A | LYS79 |
| A | GLY114 |
| A | SER115 |
| A | HOH228 |
| A | HOH298 |
| A | HOH596 |
| A | HOH597 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 226 |
| Chain | Residue |
| B | LEU208 |
| C | ASN191 |
| C | GLY197 |
| C | PRO210 |
| C | HOH279 |
| C | HOH737 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 227 |
| Chain | Residue |
| C | ASP13 |
| C | HIS23 |
| C | TRP27 |
| C | GLY48 |
| C | ARG49 |
| C | HOH568 |
| C | HOH734 |
