3JU8
Crystal Structure of Succinylglutamic Semialdehyde Dehydrogenase from Pseudomonas aeruginosa.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0006527 | biological_process | arginine catabolic process |
| A | 0008802 | molecular_function | betaine-aldehyde dehydrogenase activity |
| 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase activity |
| A | 0019544 | biological_process | arginine catabolic process to glutamate |
| A | 0019545 | biological_process | arginine catabolic process to succinate |
| A | 0043824 | molecular_function | succinylglutamate-semialdehyde dehydrogenase activity |
| A | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0006527 | biological_process | arginine catabolic process |
| B | 0008802 | molecular_function | betaine-aldehyde dehydrogenase activity |
| 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase activity |
| B | 0019544 | biological_process | arginine catabolic process to glutamate |
| B | 0019545 | biological_process | arginine catabolic process to succinate |
| B | 0043824 | molecular_function | succinylglutamate-semialdehyde dehydrogenase activity |
| B | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD A 501 |
| Chain | Residue |
| A | GLY144 |
| A | ARG203 |
| A | PHE220 |
| A | THR221 |
| A | GLY222 |
| A | SER223 |
| A | THR226 |
| A | GLU245 |
| A | MSE246 |
| A | GLY247 |
| A | CYS279 |
| A | PRO145 |
| A | GLU377 |
| A | PHE379 |
| A | PHE444 |
| A | SIN504 |
| A | HOH514 |
| A | HOH590 |
| A | HOH689 |
| A | HOH691 |
| A | HOH719 |
| A | HOH984 |
| A | TYR146 |
| A | ASN147 |
| A | LEU152 |
| A | LYS170 |
| A | PRO171 |
| A | SER172 |
| A | GLU173 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| A | ARG77 |
| A | HOH573 |
| A | HOH994 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 503 |
| Chain | Residue |
| A | SER102 |
| A | ASN105 |
| A | HOH693 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SIN A 504 |
| Chain | Residue |
| A | ASN147 |
| A | PHE148 |
| A | ARG278 |
| A | CYS279 |
| A | THR280 |
| A | GLY437 |
| A | ALA438 |
| A | NAD501 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 505 |
| Chain | Residue |
| A | ASP390 |
| A | PHE391 |
| A | ARG416 |
| A | HOH860 |
| A | HOH911 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 506 |
| Chain | Residue |
| A | SER413 |
| A | ARG414 |
| A | GLU415 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 507 |
| Chain | Residue |
| A | PRO53 |
| A | ARG57 |
| A | HOH534 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 508 |
| Chain | Residue |
| A | ASP261 |
| A | HOH983 |
| B | LEU482 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 509 |
| Chain | Residue |
| A | PHE114 |
| A | ARG115 |
| A | GLY119 |
| A | GLU120 |
| A | HOH947 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 510 |
| Chain | Residue |
| A | THR306 |
| A | LEU307 |
| A | HOH954 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 511 |
| Chain | Residue |
| A | GLN289 |
| A | GLY290 |
| A | ASP294 |
| A | ARG387 |
| A | HOH757 |
| A | HOH908 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 512 |
| Chain | Residue |
| A | ASP375 |
| A | ALA400 |
| A | THR401 |
| A | HOH818 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 488 |
| Chain | Residue |
| A | HIS231 |
| A | ASN452 |
| A | ARG454 |
| A | HOH613 |
| A | HOH703 |
| A | HOH758 |
| B | HIS231 |
| B | ASN452 |
| B | ARG454 |
| B | HOH924 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 489 |
| Chain | Residue |
| A | LEU482 |
| B | ASP261 |
| B | HOH645 |
| site_id | BC6 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD B 501 |
| Chain | Residue |
| B | THR221 |
| B | GLY222 |
| B | SER223 |
| B | THR226 |
| B | GLU245 |
| B | MSE246 |
| B | GLY247 |
| B | CYS279 |
| B | GLU377 |
| B | PHE379 |
| B | PHE444 |
| B | HOH607 |
| B | HOH636 |
| B | HOH639 |
| B | HOH642 |
| B | HOH663 |
| B | HOH671 |
| B | HOH901 |
| B | PHE143 |
| B | GLY144 |
| B | PRO145 |
| B | TYR146 |
| B | ASN147 |
| B | LEU152 |
| B | LYS170 |
| B | PRO171 |
| B | SER172 |
| B | ARG203 |
| B | PHE220 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 502 |
| Chain | Residue |
| A | GLN10 |
| B | ARG77 |
| B | LYS184 |
| B | HOH635 |
| B | HOH745 |
| B | HOH896 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 503 |
| Chain | Residue |
| B | SER102 |
| B | ASN105 |
| B | HOH599 |
| B | HOH637 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 504 |
| Chain | Residue |
| B | PRO53 |
| B | ARG57 |
| B | HOH842 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 505 |
| Chain | Residue |
| B | THR280 |
| B | GLY437 |
| B | HOH927 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 506 |
| Chain | Residue |
| B | ARG414 |
| B | GLU415 |
| B | HOH893 |
| site_id | CC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 509 |
| Chain | Residue |
| B | PHE114 |
| B | ARG115 |
| B | GLY119 |
| B | GLU120 |
| B | HOH619 |
| B | HOH699 |
| B | HOH861 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 510 |
| Chain | Residue |
| B | HOH630 |
| B | HOH631 |
| B | HOH632 |
| B | HOH633 |
| B | HOH896 |
| B | HOH904 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FiSAGQRCTCAR |
| Chain | Residue | Details |
| A | PHE272-ARG283 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LEMGGNNP |
| Chain | Residue | Details |
| A | LEU244-PRO251 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU245 | |
| A | CYS279 | |
| B | GLU245 | |
| B | CYS279 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY222 | |
| B | GLY222 |
