4KNA
Crystal structure of an N-succinylglutamate 5-semialdehyde dehydrogenase from Burkholderia thailandensis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0006527 | biological_process | L-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 | L-arginine catabolic process to L-glutamate |
| A | 0019545 | biological_process | L-arginine catabolic process to succinate |
| A | 0043824 | molecular_function | succinylglutamate-semialdehyde dehydrogenase activity |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0006527 | biological_process | L-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 | L-arginine catabolic process to L-glutamate |
| B | 0019545 | biological_process | L-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 | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01174","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01174","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
