6X9A
Structure of proline utilization A with trans-4-hydroxy-D-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 | 0006561 | biological_process | proline biosynthetic 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 |
| 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 | 0006561 | biological_process | proline biosynthetic 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 |
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 | HOH2351 |
| A | HOH2548 |
| A | HOH2831 |
| A | HOH2914 |
| A | GLN340 |
| A | TYR342 |
| A | ARG367 |
| A | VAL369 |
| A | LYS370 |
| A | GLY371 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue FMT A 2002 |
| Chain | Residue |
| A | ARG40 |
| A | ALA387 |
| A | ASP552 |
| A | HOH2215 |
| A | HOH2440 |
| A | HOH2497 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 2003 |
| Chain | Residue |
| A | GLY542 |
| A | ARG545 |
| A | THR546 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue UY7 A 2004 |
| Chain | Residue |
| A | GLU674 |
| A | PHE708 |
| A | ARG843 |
| A | SER845 |
| A | GLY1002 |
| A | ALA1003 |
| A | PHE1010 |
| A | HOH2331 |
| A | HOH2395 |
| A | HOH2472 |
| A | HOH2769 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue UY7 A 2005 |
| Chain | Residue |
| A | TRP574 |
| A | THR575 |
| A | ARG744 |
| A | HOH2189 |
| A | HOH2955 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 2006 |
| Chain | Residue |
| A | GLY1079 |
| A | HIS1097 |
| A | HOH2139 |
| A | HOH2377 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 2007 |
| Chain | Residue |
| A | ARG688 |
| A | PRO1039 |
| A | GLN1040 |
| A | HOH2235 |
| A | HOH2268 |
| A | HOH2604 |
| A | HOH2892 |
| B | SER94 |
| B | ARG170 |
| 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 | 3 |
| Details | binding site for residue SO4 A 2009 |
| Chain | Residue |
| A | ARG69 |
| A | ILE510 |
| A | ASP511 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 2010 |
| Chain | Residue |
| A | SER137 |
| A | GLN853 |
| A | GLU854 |
| A | ASP855 |
| A | ARG952 |
| A | ARG953 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 2011 |
| Chain | Residue |
| A | SER157 |
| A | ARG1091 |
| A | HOH2271 |
| A | HOH2577 |
| A | HOH2977 |
| site_id | AD3 |
| Number of Residues | 33 |
| Details | binding site for residue FAD B 2001 |
| Chain | Residue |
| B | TYR373 |
| B | TRP374 |
| B | PHE392 |
| B | THR393 |
| B | ARG394 |
| B | LYS395 |
| B | THR398 |
| B | THR422 |
| B | HIS423 |
| B | ASN424 |
| B | CYS448 |
| B | LEU449 |
| B | TYR473 |
| B | GLU492 |
| B | ASN493 |
| B | SER497 |
| B | SER498 |
| B | PHE499 |
| B | ILE1232 |
| B | GLY1233 |
| B | HOH2659 |
| B | HOH2716 |
| B | HOH2814 |
| B | ASP306 |
| B | ALA307 |
| B | VAL338 |
| B | GLN340 |
| B | TYR342 |
| B | ARG367 |
| B | VAL369 |
| B | LYS370 |
| B | GLY371 |
| B | ALA372 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue PGE B 2002 |
| Chain | Residue |
| B | GLY1079 |
| B | HIS1097 |
| B | HOH2151 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 2003 |
| Chain | Residue |
| B | GLY542 |
| B | ASP543 |
| B | THR546 |
| B | ARG687 |
| site_id | AD6 |
| Number of Residues | 10 |
| Details | binding site for residue UY7 B 2004 |
| Chain | Residue |
| B | GLU674 |
| B | PHE708 |
| B | ARG843 |
| B | SER845 |
| B | GLY1002 |
| B | ALA1003 |
| B | PHE1010 |
| B | HOH2304 |
| B | HOH2574 |
| B | HOH2740 |
| site_id | AD7 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 B 2005 |
| Chain | Residue |
| A | SER94 |
| A | ARG170 |
| B | ARG688 |
| B | PRO1039 |
| B | GLN1040 |
| B | HOH2336 |
| B | HOH2398 |
| B | HOH2713 |
| B | HOH2889 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 2006 |
| Chain | Residue |
| B | ARG202 |
| B | HOH2120 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 2007 |
| Chain | Residue |
| B | ARG69 |
| B | SER509 |
| B | ILE510 |
| B | ASP511 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 2008 |
| Chain | Residue |
| B | GLN853 |
| B | ASP855 |
| B | ARG952 |
| B | ARG953 |
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 |
