2PBZ
Crystal structure of an IMP biosynthesis protein PurP from Thermococcus kodakaraensis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006188 | biological_process | IMP biosynthetic process |
| A | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006188 | biological_process | IMP biosynthetic process |
| B | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006188 | biological_process | IMP biosynthetic process |
| C | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP A 400 |
| Chain | Residue |
| A | PHE129 |
| A | ILE263 |
| A | HOH409 |
| A | HOH436 |
| A | HOH438 |
| A | HOH454 |
| C | ARG201 |
| A | GLU145 |
| A | ARG164 |
| A | PHE165 |
| A | ILE166 |
| A | TYR170 |
| A | TYR172 |
| A | LEU194 |
| A | TYR209 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP B 400 |
| Chain | Residue |
| A | ARG201 |
| B | PHE129 |
| B | GLU145 |
| B | ARG164 |
| B | PHE165 |
| B | ILE166 |
| B | TYR170 |
| B | TYR172 |
| B | LEU194 |
| B | TYR209 |
| B | ILE263 |
| B | HOH405 |
| B | HOH427 |
| B | HOH439 |
| B | HOH441 |
| B | HOH458 |
| B | HOH470 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP C 400 |
| Chain | Residue |
| B | ARG201 |
| C | PHE129 |
| C | GLU145 |
| C | ARG164 |
| C | PHE165 |
| C | ILE166 |
| C | TYR170 |
| C | TYR172 |
| C | LEU194 |
| C | TYR209 |
| C | ILE263 |
| C | HOH404 |
| C | HOH414 |
| C | HOH415 |
| C | HOH428 |
| C | HOH433 |
| C | HOH438 |
| C | HOH457 |
