6X9D
Structure of proline utilization A with trans-4-hydroxy-L-proline bound in the L-glutamate-gamma-semialdehyde 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 | 34 |
| 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 | GLU492 |
| A | SER498 |
| A | PHE499 |
| A | ILE1232 |
| A | VAL338 |
| A | GLY1233 |
| A | HOH2374 |
| A | HOH2442 |
| A | HOH2867 |
| A | HOH2888 |
| A | GLN340 |
| A | TYR342 |
| A | ARG367 |
| A | VAL369 |
| A | LYS370 |
| A | GLY371 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue HYP A 2002 |
| Chain | Residue |
| A | GLU674 |
| A | PHE708 |
| A | ILE712 |
| A | ARG843 |
| A | SER845 |
| A | GLY1002 |
| A | ALA1003 |
| A | PHE1010 |
| A | HOH2164 |
| A | HOH2342 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue PGE A 2003 |
| Chain | Residue |
| A | HIS1045 |
| A | GLY1079 |
| A | LEU1096 |
| A | HIS1097 |
| A | HOH2687 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue FMT A 2004 |
| Chain | Residue |
| A | ARG40 |
| A | LEU386 |
| A | ALA387 |
| A | HOH2112 |
| A | HOH2376 |
| A | HOH2416 |
| A | HOH2444 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | binding site for residue NAD A 2005 |
| 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 | MG2010 |
| A | HOH2130 |
| A | HOH2264 |
| A | HOH2319 |
| A | HOH2366 |
| A | HOH2429 |
| B | HOH2132 |
| B | HOH2616 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 A 2006 |
| Chain | Residue |
| A | ARG688 |
| A | PRO1039 |
| A | GLN1040 |
| A | HOH2289 |
| A | HOH2373 |
| A | HOH2408 |
| A | HOH2754 |
| B | SER94 |
| B | GLN96 |
| B | ARG170 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 2007 |
| Chain | Residue |
| A | SER509 |
| A | ILE510 |
| A | ASP511 |
| A | ARG69 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 2008 |
| Chain | Residue |
| A | SER1194 |
| A | GLY1196 |
| A | ARG1200 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 2009 |
| Chain | Residue |
| A | SER137 |
| A | GLN853 |
| A | GLU854 |
| A | ASP855 |
| A | ARG952 |
| A | ARG953 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 2010 |
| Chain | Residue |
| A | NAD2005 |
| A | HOH2130 |
| A | HOH2275 |
| A | HOH2429 |
| B | HOH2132 |
| site_id | AD2 |
| Number of Residues | 35 |
| Details | binding site for residue FAD B 2001 |
| 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 | GLN447 |
| B | CYS448 |
| B | LEU449 |
| B | TYR473 |
| B | GLU492 |
| B | ASN493 |
| B | SER497 |
| B | SER498 |
| B | PHE499 |
| B | ILE1232 |
| B | GLY1233 |
| B | HOH2319 |
| B | HOH2373 |
| B | HOH2452 |
| site_id | AD3 |
| Number of Residues | 11 |
| Details | binding site for residue HYP B 2002 |
| Chain | Residue |
| B | GLU674 |
| B | PHE708 |
| B | ILE712 |
| B | ARG843 |
| B | SER845 |
| B | GLY1002 |
| B | ALA1003 |
| B | PHE1010 |
| B | HOH2197 |
| B | HOH2324 |
| B | HOH2421 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue PGE B 2003 |
| Chain | Residue |
| B | HIS1045 |
| B | GLY1079 |
| B | ASP1081 |
| B | LEU1096 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue PEG B 2004 |
| Chain | Residue |
| A | ALA407 |
| A | ALA411 |
| A | MET434 |
| B | LYS897 |
| B | ARG939 |
| B | HOH2646 |
| B | HOH2858 |
| site_id | AD6 |
| Number of Residues | 34 |
| Details | binding site for residue NAD B 2005 |
| 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 | MG2008 |
| B | HOH2101 |
| B | HOH2191 |
| B | HOH2270 |
| B | HOH2316 |
| B | HOH2443 |
| B | HOH2546 |
| B | HOH2739 |
| B | HOH2846 |
| B | HOH2904 |
| site_id | AD7 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 B 2006 |
| Chain | Residue |
| A | SER94 |
| A | GLN96 |
| A | ARG170 |
| B | ARG688 |
| B | PRO1039 |
| B | GLN1040 |
| B | HOH2350 |
| B | HOH2470 |
| B | HOH2697 |
| B | HOH2749 |
| site_id | AD8 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 B 2007 |
| Chain | Residue |
| B | HOH2108 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 2008 |
| Chain | Residue |
| B | NAD2005 |
| B | HOH2270 |
| B | HOH2546 |
| B | HOH2739 |
| B | HOH2846 |
| B | HOH2993 |
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 |
