2AMF
Crystal structure of 1-Pyrroline-5-Carboxylate Reductase from Human Pathogen Streptococcus Pyogenes
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006561 | biological_process | proline biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0055129 | biological_process | L-proline biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006561 | biological_process | proline biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0055129 | biological_process | L-proline biosynthetic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006561 | biological_process | proline biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0055129 | biological_process | L-proline biosynthetic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006561 | biological_process | proline biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0055129 | biological_process | L-proline biosynthetic process |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006561 | biological_process | proline biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0055129 | biological_process | L-proline biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 850 |
| Chain | Residue |
| A | GLY89 |
| A | ALA253 |
| A | LYS254 |
| A | LEU256 |
| A | HOH4334 |
| A | HOH4412 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 851 |
| Chain | Residue |
| B | LEU256 |
| B | HOH4335 |
| B | HOH4394 |
| B | GLY89 |
| B | ALA253 |
| B | LYS254 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 852 |
| Chain | Residue |
| C | GLY89 |
| C | ALA253 |
| C | LYS254 |
| C | LEU256 |
| C | HOH4332 |
| C | HOH4411 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA D 853 |
| Chain | Residue |
| D | GLY89 |
| D | ARG94 |
| D | ALA253 |
| D | LYS254 |
| D | LEU256 |
| D | HOH4485 |
| D | HOH4486 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA E 854 |
| Chain | Residue |
| E | GLY89 |
| E | ARG94 |
| E | ALA253 |
| E | LYS254 |
| E | LEU256 |
| E | HOH4412 |
| E | HOH4419 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PRO D 4240 |
| Chain | Residue |
| A | MET11 |
| A | MET86 |
| A | MET109 |
| A | PRO110 |
| A | MET112 |
| A | HOH4353 |
| D | PRO4330 |
| D | HOH4465 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PRO D 4330 |
| Chain | Residue |
| A | GLY163 |
| A | SER164 |
| D | ILE219 |
| D | SER221 |
| D | GLY224 |
| D | THR225 |
| D | THR226 |
| D | PRO4240 |
| D | HOH4389 |
| D | HOH4401 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PRO C 4241 |
| Chain | Residue |
| B | MET11 |
| B | MET109 |
| B | PRO110 |
| C | SER221 |
| C | PRO4331 |
| C | HOH4384 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PRO C 4331 |
| Chain | Residue |
| B | GLY163 |
| C | ILE219 |
| C | SER221 |
| C | GLY224 |
| C | THR225 |
| C | THR226 |
| C | PRO4241 |
| C | HOH4371 |
| C | HOH4414 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PRO B 4242 |
| Chain | Residue |
| B | ILE219 |
| B | SER221 |
| B | PRO4332 |
| B | HOH4409 |
| C | MET11 |
| C | MET86 |
| C | MET109 |
| C | PRO110 |
| C | MET112 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PRO B 4332 |
| Chain | Residue |
| B | ILE219 |
| B | SER221 |
| B | GLY224 |
| B | THR225 |
| B | THR226 |
| B | PRO4242 |
| B | HOH4393 |
| B | HOH4396 |
| C | GLY163 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PRO A 4243 |
| Chain | Residue |
| A | SER221 |
| A | PRO4333 |
| A | HOH4377 |
| D | MET11 |
| D | MET86 |
| D | MET109 |
| D | PRO110 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PRO A 4333 |
| Chain | Residue |
| D | SER164 |
| A | ILE219 |
| A | SER221 |
| A | GLY224 |
| A | THR225 |
| A | THR226 |
| A | PRO4243 |
| A | HOH4352 |
| A | HOH4401 |
| D | GLY163 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PRO E 4244 |
| Chain | Residue |
| E | MET11 |
| E | MET109 |
| E | PRO110 |
| E | MET112 |
| E | ILE219 |
| E | SER221 |
| E | PRO4334 |
| E | HOH4339 |
| E | HOH4406 |
| E | HOH4426 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PRO E 4334 |
| Chain | Residue |
| E | GLY163 |
| E | ILE219 |
| E | SER221 |
| E | GLY224 |
| E | THR225 |
| E | THR226 |
| E | PRO4244 |
| E | HOH4380 |
| E | HOH4415 |
