4LEM
Crystal structure of the Delta-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| A | 0004657 | molecular_function | proline dehydrogenase activity |
| A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| A | 0010133 | biological_process | obsolete L-proline catabolic process to L-glutamate |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| B | 0004657 | molecular_function | proline dehydrogenase activity |
| B | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| B | 0010133 | biological_process | obsolete L-proline catabolic process to L-glutamate |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| C | 0004657 | molecular_function | proline dehydrogenase activity |
| C | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| C | 0010133 | biological_process | obsolete L-proline catabolic process to L-glutamate |
| C | 0016491 | molecular_function | oxidoreductase activity |
| D | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| D | 0004657 | molecular_function | proline dehydrogenase activity |
| D | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| D | 0010133 | biological_process | obsolete L-proline catabolic process to L-glutamate |
| D | 0016491 | molecular_function | oxidoreductase activity |
| E | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| E | 0004657 | molecular_function | proline dehydrogenase activity |
| E | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| E | 0010133 | biological_process | obsolete L-proline catabolic process to L-glutamate |
| E | 0016491 | molecular_function | oxidoreductase activity |
| F | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| F | 0004657 | molecular_function | proline dehydrogenase activity |
| F | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| F | 0010133 | biological_process | obsolete L-proline catabolic process to L-glutamate |
| F | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE B12 A 601 |
| Chain | Residue |
| A | PHE246 |
| A | HOH737 |
| A | HOH738 |
| A | HOH769 |
| A | HOH773 |
| A | HOH792 |
| A | HOH887 |
| A | HOH912 |
| A | HOH969 |
| A | HOH1066 |
| A | HOH1068 |
| A | ASP250 |
| A | HOH1082 |
| A | HOH1108 |
| A | HOH1180 |
| C | GLU383 |
| C | LYS386 |
| C | GLU398 |
| C | TYR399 |
| C | HOH844 |
| A | ALA268 |
| A | THR269 |
| A | HIS272 |
| A | ARG373 |
| A | HOH709 |
| A | HOH711 |
| A | HOH720 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE B12 B 601 |
| Chain | Residue |
| B | PHE246 |
| B | ASP250 |
| B | ALA268 |
| B | THR269 |
| B | HIS272 |
| B | ARG373 |
| B | HOH706 |
| B | HOH735 |
| B | HOH791 |
| B | HOH830 |
| B | HOH841 |
| B | HOH870 |
| B | HOH986 |
| B | HOH1123 |
| B | HOH1148 |
| C | ASP37 |
| C | PRO39 |
| C | HOH829 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE B12 C 601 |
| Chain | Residue |
| C | ILE186 |
| C | PHE246 |
| C | ASP250 |
| C | THR269 |
| C | HIS272 |
| C | HOH780 |
| C | HOH792 |
| C | HOH819 |
| C | HOH842 |
| C | HOH851 |
| C | HOH961 |
| C | HOH1106 |
| D | ASN280 |
| D | ARG283 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 602 |
| Chain | Residue |
| C | ALA385 |
| C | LYS386 |
| C | ALA388 |
| C | VAL391 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE B12 D 601 |
| Chain | Residue |
| C | ALA79 |
| C | ASP250 |
| C | VAL251 |
| C | ALA254 |
| C | HOH907 |
| D | ILE186 |
| D | PHE246 |
| D | ASP250 |
| D | THR269 |
| D | HIS272 |
| D | HOH720 |
| D | HOH741 |
| D | HOH742 |
| D | HOH785 |
| D | HOH794 |
| D | HOH809 |
| D | HOH822 |
| D | HOH884 |
| D | HOH949 |
| D | HOH964 |
| D | HOH977 |
| D | HOH995 |
| D | HOH1023 |
| D | HOH1129 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 602 |
| Chain | Residue |
| D | ALA385 |
| D | LYS386 |
| D | ALA388 |
| D | VAL391 |
| D | HOH828 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F 601 |
| Chain | Residue |
| F | ALA385 |
| F | LYS386 |
| F | ALA388 |
| F | VAL391 |
| F | HOH795 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FdYQGQKCSAVS |
| Chain | Residue | Details |
| A | PHE320-SER331 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GETGGKDF |
| Chain | Residue | Details |
| A | GLY292-PHE299 |
