1EYY
CRYSTAL STRUCTURE OF THE NADP+ DEPENDENT ALDEHYDE DEHYDROGENASE FROM VIBRIO HARVEYI.
Replaces: 1CBZFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0033721 | molecular_function | aldehyde dehydrogenase (NADP+) 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 | 0033721 | molecular_function | aldehyde dehydrogenase (NADP+) activity |
| 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 |
| C | 0033721 | molecular_function | aldehyde dehydrogenase (NADP+) activity |
| 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 |
| D | 0033721 | molecular_function | aldehyde dehydrogenase (NADP+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NAP A 650 |
| Chain | Residue |
| A | SER146 |
| A | LYS172 |
| A | HIS174 |
| A | THR175 |
| A | ARG210 |
| A | GLN214 |
| A | PHE227 |
| A | GLY229 |
| A | SER230 |
| A | GLY233 |
| A | LEU237 |
| A | HOH1030 |
| A | HOH1411 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NAP B 750 |
| Chain | Residue |
| A | ASP6 |
| B | SER146 |
| B | LYS172 |
| B | HIS174 |
| B | THR175 |
| B | ARG210 |
| B | GLN214 |
| B | PHE227 |
| B | SER230 |
| B | GLY233 |
| B | HOH1070 |
| B | HOH1412 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NAP C 850 |
| Chain | Residue |
| C | SER146 |
| C | LYS172 |
| C | HIS174 |
| C | THR175 |
| C | ARG210 |
| C | GLN214 |
| C | PHE227 |
| C | GLY229 |
| C | SER230 |
| C | GLY233 |
| C | LEU237 |
| C | HOH1110 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE NAP D 950 |
| Chain | Residue |
| D | SER146 |
| D | LYS172 |
| D | HIS174 |
| D | THR175 |
| D | ARG210 |
| D | GLN214 |
| D | PHE227 |
| D | SER230 |
| D | GLY233 |
| D | HOH1150 |
| D | HOH1413 |
| site_id | CTA |
| Number of Residues | 2 |
| Details | THE KEY RESIDUES AROUND THE ACTIVE SITE |
| Chain | Residue |
| A | GLU253 |
| A | CYS289 |
| site_id | CTB |
| Number of Residues | 2 |
| Details | THE KEY RESIDUES AROUND THE ACTIVE SITE |
| Chain | Residue |
| B | GLU253 |
| B | CYS289 |
| site_id | CTC |
| Number of Residues | 2 |
| Details | THE KEY RESIDUES AROUND THE ACTIVE SITE |
| Chain | Residue |
| C | GLU253 |
| C | CYS289 |
| site_id | CTD |
| Number of Residues | 2 |
| Details | THE KEY RESIDUES AROUND THE ACTIVE SITE |
| Chain | Residue |
| D | GLU253 |
| D | CYS289 |
| site_id | NPA |
| Number of Residues | 4 |
| Details | KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR |
| Chain | Residue |
| A | LYS172 |
| A | THR175 |
| A | ARG210 |
| A | GLU377 |
| site_id | NPB |
| Number of Residues | 4 |
| Details | KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR |
| Chain | Residue |
| B | THR175 |
| B | ARG210 |
| B | GLU377 |
| B | LYS172 |
| site_id | NPC |
| Number of Residues | 4 |
| Details | KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR |
| Chain | Residue |
| C | LYS172 |
| C | THR175 |
| C | ARG210 |
| C | GLU377 |
| site_id | NPD |
| Number of Residues | 4 |
| Details | KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR |
| Chain | Residue |
| D | LYS172 |
| D | THR175 |
| D | ARG210 |
| D | GLU377 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | GLU253 | |
| A | CYS289 | |
| B | GLU253 | |
| B | CYS289 | |
| C | GLU253 | |
| C | CYS289 | |
| D | GLU253 | |
| D | CYS289 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY229 | |
| B | GLY229 | |
| C | GLY229 | |
| D | GLY229 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| A | CYS289 | |
| A | ASN147 | |
| A | GLU253 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| B | CYS289 | |
| B | ASN147 | |
| B | GLU253 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| C | CYS289 | |
| C | ASN147 | |
| C | GLU253 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| D | CYS289 | |
| D | ASN147 | |
| D | GLU253 |
