7MYB
Structure of proline utilization A with tetrahydrothiophene-2-carboxylate bound in the proline dehydrogenase active site
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| A | 0004657 | molecular_function | proline dehydrogenase activity |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0006560 | biological_process | proline metabolic process |
| A | 0006562 | biological_process | L-proline catabolic process |
| A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| A | 0010133 | biological_process | L-proline catabolic process to L-glutamate |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0055129 | biological_process | L-proline biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| B | 0004657 | molecular_function | proline dehydrogenase activity |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0006560 | biological_process | proline metabolic process |
| B | 0006562 | biological_process | L-proline catabolic process |
| B | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| B | 0010133 | biological_process | L-proline catabolic process to L-glutamate |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0055129 | biological_process | L-proline biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue UJM A 1301 |
| Chain | Residue |
| A | LYS265 |
| A | ASP306 |
| A | TYR473 |
| A | TYR485 |
| A | ARG488 |
| A | ARG489 |
| A | UJP1302 |
| A | FAD1304 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue UJP A 1302 |
| Chain | Residue |
| A | ASP306 |
| A | TYR473 |
| A | TYR485 |
| A | ARG488 |
| A | ARG489 |
| A | UJM1301 |
| A | FAD1304 |
| A | LYS265 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue PGE A 1303 |
| Chain | Residue |
| A | LEU1078 |
| A | GLY1079 |
| A | ASP1081 |
| A | THR1095 |
| A | LEU1096 |
| A | HOH1615 |
| site_id | AC4 |
| Number of Residues | 37 |
| Details | binding site for residue FAD A 1304 |
| Chain | Residue |
| A | ASP306 |
| A | ALA307 |
| A | VAL338 |
| A | GLN340 |
| A | TYR342 |
| A | ARG367 |
| A | VAL369 |
| A | LYS370 |
| A | GLY371 |
| A | ALA372 |
| A | TYR373 |
| A | TRP374 |
| A | PHE392 |
| A | THR393 |
| A | ARG394 |
| A | LYS395 |
| A | THR398 |
| A | ALA421 |
| A | THR422 |
| A | HIS423 |
| A | ASN424 |
| A | CYS448 |
| A | LEU449 |
| A | TYR473 |
| A | ARG489 |
| A | GLU492 |
| A | SER497 |
| A | SER498 |
| A | PHE499 |
| A | ILE1232 |
| A | GLY1233 |
| A | UJM1301 |
| A | UJP1302 |
| A | HOH1443 |
| A | HOH1462 |
| A | HOH1617 |
| A | HOH2189 |
| site_id | AC5 |
| Number of Residues | 35 |
| Details | binding site for residue NAD A 1305 |
| Chain | Residue |
| A | ILE703 |
| A | SER704 |
| A | PRO705 |
| A | TRP706 |
| A | ASN707 |
| A | ILE712 |
| A | LYS730 |
| A | ALA732 |
| A | GLU733 |
| A | GLY763 |
| A | GLY766 |
| A | ALA767 |
| A | PHE780 |
| A | THR781 |
| A | GLY782 |
| A | SER783 |
| A | VAL786 |
| A | GLU810 |
| A | THR811 |
| A | GLY812 |
| A | CYS844 |
| A | GLU940 |
| A | PHE942 |
| A | PHE1010 |
| A | MG1309 |
| A | HOH1406 |
| A | HOH1502 |
| A | HOH1554 |
| A | HOH1638 |
| A | HOH1824 |
| A | HOH1827 |
| A | HOH2076 |
| A | HOH2094 |
| A | HOH2095 |
| A | HOH2220 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 1306 |
| Chain | Residue |
| A | HOH1890 |
| A | HOH2194 |
| B | SER94 |
| B | ARG170 |
| A | ARG688 |
| A | PRO1039 |
| A | GLN1040 |
| A | HOH1558 |
| A | HOH1575 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 1307 |
| Chain | Residue |
| A | SER1194 |
| A | GLY1196 |
| A | ARG1200 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 1308 |
| Chain | Residue |
| A | LYS1060 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 1309 |
| Chain | Residue |
| A | NAD1305 |
| A | HOH1502 |
| A | HOH1623 |
| A | HOH1824 |
| A | HOH2095 |
| B | HOH2244 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue UJM B 1301 |
| Chain | Residue |
| B | LYS265 |
| B | TYR473 |
| B | ARG488 |
| B | UJP1302 |
| B | FAD1304 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue UJP B 1302 |
| Chain | Residue |
| B | LYS265 |
| B | ASP306 |
| B | TYR473 |
| B | ARG488 |
| B | UJM1301 |
| B | FAD1304 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue PGE B 1303 |
| Chain | Residue |
| B | HIS1045 |
| B | GLY1079 |
| B | LEU1096 |
| B | HIS1097 |
| B | HOH1431 |
| B | HOH1669 |
| site_id | AD4 |
| Number of Residues | 33 |
| Details | binding site for residue FAD B 1304 |
| Chain | Residue |
| B | ASP306 |
| B | ALA307 |
| B | VAL338 |
| B | GLN340 |
| B | TYR342 |
| B | ARG367 |
| B | VAL369 |
| B | LYS370 |
| B | GLY371 |
| B | ALA372 |
| B | TYR373 |
| B | TRP374 |
| B | PHE392 |
| B | THR393 |
| B | ARG394 |
| B | LYS395 |
| B | THR398 |
| B | ALA421 |
| B | THR422 |
| B | HIS423 |
| B | ASN424 |
| B | CYS448 |
| B | LEU449 |
| B | TYR473 |
| B | GLU492 |
| B | SER498 |
| B | PHE499 |
| B | ILE1232 |
| B | UJM1301 |
| B | UJP1302 |
| B | HOH1487 |
| B | HOH1556 |
| B | HOH2149 |
| site_id | AD5 |
| Number of Residues | 34 |
| Details | binding site for residue NAD B 1305 |
| Chain | Residue |
| B | ILE703 |
| B | SER704 |
| B | PRO705 |
| B | TRP706 |
| B | ASN707 |
| B | ILE712 |
| B | LYS730 |
| B | ALA732 |
| B | GLU733 |
| B | GLY763 |
| B | GLY766 |
| B | ALA767 |
| B | PHE780 |
| B | THR781 |
| B | GLY782 |
| B | SER783 |
| B | VAL786 |
| B | GLU810 |
| B | THR811 |
| B | GLY812 |
| B | CYS844 |
| B | GLU940 |
| B | PHE942 |
| B | PHE1010 |
| B | MG1307 |
| B | HOH1403 |
| B | HOH1508 |
| B | HOH1531 |
| B | HOH1611 |
| B | HOH1708 |
| B | HOH1824 |
| B | HOH2086 |
| B | HOH2212 |
| B | HOH2279 |
| site_id | AD6 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 B 1306 |
| Chain | Residue |
| A | SER94 |
| A | ARG170 |
| B | ARG688 |
| B | PRO1039 |
| B | GLN1040 |
| B | HOH1503 |
| B | HOH1717 |
| B | HOH2184 |
| B | HOH2220 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 1307 |
| Chain | Residue |
| B | NAD1305 |
| B | HOH1531 |
| B | HOH1824 |
| B | HOH2086 |
| B | HOH2212 |
| B | HOH2453 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 1308 |
| Chain | Residue |
| B | GLU674 |
| B | PHE708 |
| B | ALA711 |
| B | HOH1696 |
| B | HOH2071 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FdSAGQRCSALR |
| Chain | Residue | Details |
| A | PHE837-ARG848 |
