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 |