4KNA
Crystal structure of an N-succinylglutamate 5-semialdehyde dehydrogenase from Burkholderia thailandensis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
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 | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) 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 | 3 |
Details | BINDING SITE FOR RESIDUE CL A 501 |
Chain | Residue |
A | ARG420 |
A | HOH996 |
B | ARG134 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 502 |
Chain | Residue |
A | THR400 |
A | ALA401 |
A | PHE402 |
A | ARG424 |
A | GLY447 |
A | CA504 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 503 |
Chain | Residue |
A | ARG282 |
A | GLU375 |
A | HIS377 |
A | PHE378 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 504 |
Chain | Residue |
A | THR400 |
A | EDO502 |
A | HOH951 |
A | HOH952 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 501 |
Chain | Residue |
A | ARG134 |
A | MET467 |
B | ARG420 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 502 |
Chain | Residue |
B | ARG282 |
B | ALA334 |
B | HIS377 |
B | PHE378 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 503 |
Chain | Residue |
B | THR400 |
B | ALA401 |
B | PHE402 |
B | ARG424 |
B | CA504 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA B 504 |
Chain | Residue |
B | THR400 |
B | EDO503 |
B | HOH678 |
B | HOH1035 |
Functional Information from PROSITE/UniProt
site_id | PS00070 |
Number of Residues | 12 |
Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FlSAGQRCTCAR |
Chain | Residue | Details |
A | PHE271-ARG282 |
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LEMGGNNP |
Chain | Residue | Details |
A | LEU243-PRO250 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01174 |
Chain | Residue | Details |
A | GLU244 | |
A | CYS278 | |
B | GLU244 | |
B | CYS278 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01174 |
Chain | Residue | Details |
A | GLY221 | |
B | GLY221 |