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 | 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 | 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 |