3EFV
Crystal Structure of a Putative Succinate-Semialdehyde Dehydrogenase from Salmonella typhimurium LT2 with bound NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
| A | 0004777 | molecular_function | succinate-semialdehyde dehydrogenase (NAD+) activity |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0009447 | biological_process | putrescine 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
| B | 0004777 | molecular_function | succinate-semialdehyde dehydrogenase (NAD+) activity |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0009447 | biological_process | putrescine 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
| C | 0004777 | molecular_function | succinate-semialdehyde dehydrogenase (NAD+) activity |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0009447 | biological_process | putrescine catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
| D | 0004777 | molecular_function | succinate-semialdehyde dehydrogenase (NAD+) activity |
| D | 0006099 | biological_process | tricarboxylic acid cycle |
| D | 0009447 | biological_process | putrescine catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 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 | 28 |
| Details | BINDING SITE FOR RESIDUE NAD A 463 |
| Chain | Residue |
| A | ILE133 |
| A | ALA162 |
| A | ASN193 |
| A | VAL196 |
| A | THR211 |
| A | GLY212 |
| A | SER213 |
| A | ALA216 |
| A | ALA219 |
| A | GLU234 |
| A | LEU235 |
| A | MSE134 |
| A | GLY236 |
| A | CYS268 |
| A | ARG312 |
| A | GLU365 |
| A | PHE367 |
| A | PHE431 |
| A | HOH588 |
| A | HOH914 |
| A | HOH967 |
| A | PRO135 |
| A | TRP136 |
| A | ASN137 |
| A | GLN142 |
| A | ARG145 |
| A | LYS160 |
| A | HIS161 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD B 463 |
| Chain | Residue |
| B | ILE133 |
| B | MSE134 |
| B | PRO135 |
| B | TRP136 |
| B | ASN137 |
| B | GLN142 |
| B | ARG145 |
| B | LYS160 |
| B | ALA162 |
| B | PRO163 |
| B | ASN193 |
| B | VAL196 |
| B | THR211 |
| B | GLY212 |
| B | SER213 |
| B | ALA216 |
| B | ALA219 |
| B | GLU234 |
| B | LEU235 |
| B | GLY236 |
| B | CYS268 |
| B | GLU365 |
| B | PHE367 |
| B | PHE431 |
| B | HOH618 |
| B | HOH656 |
| B | HOH787 |
| B | HOH814 |
| B | HOH848 |
| B | HOH954 |
| B | HOH960 |
| B | HOH1024 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD C 463 |
| Chain | Residue |
| C | ILE133 |
| C | MSE134 |
| C | PRO135 |
| C | TRP136 |
| C | ASN137 |
| C | GLN142 |
| C | ARG145 |
| C | LYS160 |
| C | HIS161 |
| C | ALA162 |
| C | PRO163 |
| C | ASN193 |
| C | VAL196 |
| C | THR211 |
| C | GLY212 |
| C | SER213 |
| C | ALA216 |
| C | ALA219 |
| C | GLU234 |
| C | LEU235 |
| C | GLY236 |
| C | CYS268 |
| C | ARG312 |
| C | GLU365 |
| C | PHE367 |
| C | PHE431 |
| C | HOH710 |
| C | HOH913 |
| C | HOH918 |
| C | HOH976 |
| C | HOH1039 |
| C | HOH1056 |
| C | HOH1132 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD D 463 |
| Chain | Residue |
| D | ARG145 |
| D | LYS160 |
| D | ALA162 |
| D | PRO163 |
| D | ASN193 |
| D | VAL196 |
| D | THR211 |
| D | GLY212 |
| D | SER213 |
| D | ALA216 |
| D | ALA219 |
| D | GLU234 |
| D | LEU235 |
| D | GLY236 |
| D | CYS268 |
| D | GLU365 |
| D | PHE367 |
| D | PHE431 |
| D | HOH824 |
| D | HOH1021 |
| D | HOH1142 |
| D | HOH1300 |
| D | HOH1316 |
| D | ILE133 |
| D | MSE134 |
| D | PRO135 |
| D | TRP136 |
| D | ASN137 |
| D | GLN142 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. YqNTGQVCAAAK |
| Chain | Residue | Details |
| A | TYR261-LYS272 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| A | CYS268 | |
| A | GLU234 | |
| A | ASN137 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| B | CYS268 | |
| B | GLU234 | |
| B | ASN137 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| C | CYS268 | |
| C | GLU234 | |
| C | ASN137 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| D | CYS268 | |
| D | GLU234 | |
| D | ASN137 |
