6UFP
Structure of proline utilization A with the FAD covalently modified by L-thiazolidine-2-carboxylate and three cysteines (Cys46, Cys470, Cys638) modified to S,S-(2-HYDROXYETHYL)THIOCYSTEINE
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 | 26 |
| Details | binding site for residue NAD A 1303 |
| Chain | Residue |
| A | ILE703 |
| A | GLY763 |
| A | GLY766 |
| A | ALA767 |
| A | PHE780 |
| A | THR781 |
| A | GLY782 |
| A | SER783 |
| A | VAL786 |
| A | GLU810 |
| A | THR811 |
| A | SER704 |
| A | GLY812 |
| A | CYS844 |
| A | GLU940 |
| A | PHE942 |
| A | PHE1010 |
| A | HOH1657 |
| A | HOH1845 |
| A | PRO705 |
| A | TRP706 |
| A | ASN707 |
| A | ILE712 |
| A | LYS730 |
| A | ALA732 |
| A | GLU733 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 1304 |
| Chain | Residue |
| A | GLY1079 |
| A | LEU1096 |
| A | HIS1097 |
| A | HOH1557 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 A 1305 |
| Chain | Residue |
| A | ARG688 |
| A | PRO1039 |
| A | GLN1040 |
| A | HOH1437 |
| A | HOH1440 |
| A | HOH1886 |
| B | SER94 |
| B | GLN96 |
| B | ARG170 |
| B | HOH1492 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 1306 |
| Chain | Residue |
| A | ARG69 |
| A | SER509 |
| A | ILE510 |
| A | ASP511 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 1307 |
| Chain | Residue |
| A | SER1194 |
| A | GLY1196 |
| A | ARG1200 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 1308 |
| Chain | Residue |
| A | GLN853 |
| A | GLU854 |
| A | ASP855 |
| A | ARG952 |
| A | ARG953 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue FMT A 1309 |
| Chain | Residue |
| A | ARG40 |
| A | ALA387 |
| A | HOH1457 |
| A | HOH1458 |
| A | HOH1757 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | binding site for residue NAD B 1303 |
| Chain | Residue |
| B | ILE703 |
| B | SER704 |
| B | PRO705 |
| B | TRP706 |
| B | LYS730 |
| B | ALA732 |
| B | GLY763 |
| B | GLY766 |
| B | ALA767 |
| B | PHE780 |
| B | GLY782 |
| B | SER783 |
| B | VAL786 |
| B | THR811 |
| B | GLU940 |
| B | PHE942 |
| B | HOH1802 |
| B | HOH1814 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 1304 |
| Chain | Residue |
| B | GLY1079 |
| B | LEU1080 |
| B | LEU1096 |
| B | HIS1097 |
| B | HOH1658 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 1305 |
| Chain | Residue |
| A | SER94 |
| A | ARG170 |
| B | ARG688 |
| B | PRO1039 |
| B | GLN1040 |
| B | HOH1433 |
| B | HOH1448 |
| B | HOH1581 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 1306 |
| Chain | Residue |
| B | SER1194 |
| B | GLY1196 |
| B | ARG1200 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue FMT B 1307 |
| Chain | Residue |
| B | ARG40 |
| B | ALA387 |
| B | HOH1415 |
| B | HOH1434 |
| B | HOH1461 |
| B | HOH1462 |
| site_id | AD4 |
| Number of Residues | 30 |
| Details | binding site for residues FDA A 1301 and T2C A 1302 |
| Chain | Residue |
| 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 | TYR473 |
| A | TYR485 |
| A | ARG488 |
| A | ARG489 |
| A | SER498 |
| A | PHE499 |
| A | HOH1463 |
| A | LYS265 |
| A | ASP306 |
| site_id | AD5 |
| Number of Residues | 31 |
| Details | binding site for residues FDA B 1301 and T2C B 1302 |
| 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 | TYR373 |
| 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 | SER498 |
| B | PHE499 |
| B | HOH1555 |
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 |
| B | PHE837-ARG848 | |
| A | PHE837-ARG848 |
