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 | 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 | 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 |