6VZ9
Structure of proline utilization A with the FAD covalently modified by L-thiazolidine-2-carboxylate
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 | 0003842 | molecular_function | 1-pyrroline-5-carboxylate 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 | 0006561 | biological_process | proline biosynthetic process |
A | 0006562 | biological_process | proline catabolic process |
A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
A | 0010133 | biological_process | proline catabolic process to 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 |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003677 | molecular_function | DNA binding |
B | 0003700 | molecular_function | DNA-binding transcription factor activity |
B | 0003842 | molecular_function | 1-pyrroline-5-carboxylate 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 | 0006561 | biological_process | proline biosynthetic process |
B | 0006562 | biological_process | proline catabolic process |
B | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
B | 0010133 | biological_process | proline catabolic process to 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 34 |
Details | binding site for residue NAD A 1302 |
Chain | Residue |
A | ILE703 |
A | GLY763 |
A | GLY766 |
A | ALA767 |
A | PHE780 |
A | THR781 |
A | GLY782 |
A | SER783 |
A | VAL786 |
A | ILE790 |
A | GLU810 |
A | SER704 |
A | THR811 |
A | GLY812 |
A | CYS844 |
A | GLU940 |
A | PHE942 |
A | PHE1010 |
A | MG1303 |
A | HOH1453 |
A | HOH1478 |
A | HOH1488 |
A | PRO705 |
A | HOH1516 |
A | HOH1945 |
A | HOH1961 |
A | HOH2167 |
A | HOH2198 |
A | TRP706 |
A | ASN707 |
A | ILE712 |
A | LYS730 |
A | ALA732 |
A | GLU733 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 1303 |
Chain | Residue |
A | NAD1302 |
A | HOH1453 |
A | HOH1488 |
A | HOH1961 |
A | HOH2167 |
A | HOH2323 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue PEG A 1305 |
Chain | Residue |
A | GLY1079 |
A | THR1095 |
A | LEU1096 |
A | HIS1097 |
A | HOH1484 |
A | HOH1759 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue SO4 A 1306 |
Chain | Residue |
A | ARG688 |
A | PRO1039 |
A | GLN1040 |
A | HOH1434 |
A | HOH1535 |
A | HOH1583 |
A | HOH2123 |
B | SER94 |
B | ARG170 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 1307 |
Chain | Residue |
A | ARG69 |
A | SER509 |
A | ILE510 |
A | ASP511 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 1308 |
Chain | Residue |
A | SER137 |
A | GLN853 |
A | GLU854 |
A | ASP855 |
A | ARG952 |
A | ARG953 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 1309 |
Chain | Residue |
A | SER1194 |
A | GLY1196 |
A | ARG1200 |
A | HOH2221 |
site_id | AC8 |
Number of Residues | 33 |
Details | binding site for residue NAD B 1302 |
Chain | Residue |
B | HOH1846 |
B | HOH2073 |
B | HOH2124 |
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 | MG1303 |
B | HOH1494 |
B | HOH1501 |
B | HOH1516 |
B | HOH1695 |
B | HOH1819 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue MG B 1303 |
Chain | Residue |
B | NAD1302 |
B | HOH1494 |
B | HOH1819 |
B | HOH1846 |
B | HOH2124 |
B | HOH2393 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue PGE B 1305 |
Chain | Residue |
B | GLY1079 |
B | THR1095 |
B | HOH1602 |
site_id | AD2 |
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 | HOH1440 |
B | HOH1642 |
B | HOH1784 |
B | HOH1931 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue SO4 B 1307 |
Chain | Residue |
B | ARG803 |
B | SER1194 |
B | ARG1200 |
B | HOH1404 |
B | HOH1566 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 1308 |
Chain | Residue |
B | ARG69 |
B | SER509 |
B | ILE510 |
B | ASP511 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 1309 |
Chain | Residue |
B | ARG202 |
B | LYS206 |
B | HOH1403 |
site_id | AD6 |
Number of Residues | 38 |
Details | binding site for residues FAD A 1301 and T2C A 1304 |
Chain | Residue |
A | LYS265 |
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 | GLN447 |
A | CYS448 |
A | LEU449 |
A | TYR473 |
A | TYR485 |
A | ARG488 |
A | ARG489 |
A | GLU492 |
A | SER497 |
A | SER498 |
A | PHE499 |
A | ILE1232 |
A | GLY1233 |
A | HOH1427 |
A | HOH1521 |
A | HOH2039 |
site_id | AD7 |
Number of Residues | 37 |
Details | binding site for residues FAD B 1301 and T2C B 1304 |
Chain | Residue |
B | LYS265 |
B | ASP306 |
B | ALA307 |
B | VAL338 |
B | GLN340 |
B | TYR342 |
B | ARG367 |
B | VAL369 |
B | LYS370 |
B | GLY371 |
B | ALA372 |
B | TRP374 |
B | PHE392 |
B | THR393 |
B | ARG394 |
B | LYS395 |
B | THR398 |
B | ALA421 |
B | THR422 |
B | HIS423 |
B | ASN424 |
B | GLN447 |
B | CYS448 |
B | LEU449 |
B | TYR473 |
B | ARG488 |
B | ARG489 |
B | GLU492 |
B | SER497 |
B | SER498 |
B | PHE499 |
B | GLY1233 |
B | HOH1572 |
B | HOH1687 |
B | HOH1804 |
B | HOH1985 |
B | HOH2169 |
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 |