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 | 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 | 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 |
B | 0006525 | biological_process | arginine metabolic process |
B | 0006527 | biological_process | arginine catabolic process |
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 | 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 |
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 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
A | GLU245 | |
A | CYS279 | |
A | ASN147 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
B | GLU245 | |
B | CYS279 | |
B | ASN147 |