5KF6
Structure of proline utilization A from Sinorhizobium meliloti complexed with L-tetrahydrofuroic acid and NAD+ in space group P21
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 | 35 |
Details | binding site for residue FAD A 2001 |
Chain | Residue |
A | ASP306 |
A | ALA372 |
A | TYR373 |
A | TRP374 |
A | PHE392 |
A | THR393 |
A | ARG394 |
A | LYS395 |
A | THR398 |
A | ALA421 |
A | THR422 |
A | ALA307 |
A | HIS423 |
A | ASN424 |
A | GLN447 |
A | CYS448 |
A | LEU449 |
A | TYR473 |
A | ARG489 |
A | GLU492 |
A | SER497 |
A | SER498 |
A | VAL338 |
A | PHE499 |
A | TFB2003 |
A | HOH2128 |
A | HOH2304 |
A | HOH2364 |
A | HOH2532 |
A | GLN340 |
A | TYR342 |
A | ARG367 |
A | VAL369 |
A | LYS370 |
A | GLY371 |
site_id | AC2 |
Number of Residues | 32 |
Details | binding site for residue NAD A 2002 |
Chain | Residue |
A | ILE703 |
A | SER704 |
A | PRO705 |
A | TRP706 |
A | ASN707 |
A | ILE712 |
A | LYS730 |
A | ALA732 |
A | GLU733 |
A | ASP762 |
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 | MG2004 |
A | HOH2188 |
A | HOH2221 |
A | HOH2264 |
A | HOH2268 |
A | HOH2549 |
A | HOH2603 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue TFB A 2003 |
Chain | Residue |
A | LYS265 |
A | ASP306 |
A | TYR473 |
A | TYR485 |
A | ARG488 |
A | ARG489 |
A | FAD2001 |
A | HOH2338 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG A 2004 |
Chain | Residue |
A | NAD2002 |
A | HOH2221 |
A | HOH2276 |
A | HOH2549 |
A | HOH2651 |
B | HOH2678 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue PGE A 2005 |
Chain | Residue |
A | HIS1045 |
A | GLY1079 |
A | HIS1097 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue PGE A 2006 |
Chain | Residue |
A | ALA670 |
A | GLU671 |
A | GLU674 |
A | ALA711 |
A | ARG843 |
A | HOH2400 |
A | HOH2569 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue PGE A 2007 |
Chain | Residue |
A | LYS379 |
A | LEU383 |
A | GLU1090 |
A | ASN1219 |
A | HOH2537 |
A | HOH2562 |
site_id | AC8 |
Number of Residues | 31 |
Details | binding site for residue FAD B 2001 |
Chain | Residue |
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 | TFB2003 |
B | HOH2105 |
B | HOH2120 |
B | HOH2389 |
B | ASP306 |
B | ALA307 |
site_id | AC9 |
Number of Residues | 32 |
Details | binding site for residue NAD B 2002 |
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 | MG2004 |
B | HOH2159 |
B | HOH2251 |
B | HOH2363 |
B | HOH2563 |
B | HOH2590 |
B | HOH2597 |
B | HOH2627 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue TFB B 2003 |
Chain | Residue |
B | LYS265 |
B | ASP306 |
B | TYR473 |
B | ARG488 |
B | FAD2001 |
B | HOH2404 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue MG B 2004 |
Chain | Residue |
B | NAD2002 |
B | HOH2251 |
B | HOH2478 |
B | HOH2590 |
B | HOH2627 |
B | HOH2668 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue PGE B 2005 |
Chain | Residue |
B | ALA581 |
B | THR582 |
B | HOH2101 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue PGE B 2006 |
Chain | Residue |
B | GLU674 |
B | ALA711 |
B | ARG843 |
B | HOH2260 |
B | HOH2501 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue PGE B 2007 |
Chain | Residue |
B | HIS1045 |
B | GLY1079 |
B | LEU1096 |
B | HIS1097 |
B | HOH2140 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue PGE B 2008 |
Chain | Residue |
B | GLU73 |
B | GLY77 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue PGE B 2009 |
Chain | Residue |
B | LYS379 |
B | GLU1090 |
B | ASN1219 |
B | HOH2174 |
B | HOH2536 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue PG4 B 2010 |
Chain | Residue |
A | HIS433 |
A | MET434 |
B | LYS897 |
B | HOH2574 |
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 |