4I3V
Structure of phosphonoacetaldehyde dehydrogenase in complex with phosphonoacetaldehyde and cofactor NAD+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008911 | molecular_function | lactaldehyde dehydrogenase activity |
| 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 | 0008911 | molecular_function | lactaldehyde dehydrogenase 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0008911 | molecular_function | lactaldehyde dehydrogenase 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 |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008911 | molecular_function | lactaldehyde dehydrogenase 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 |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0008911 | molecular_function | lactaldehyde dehydrogenase activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0008911 | molecular_function | lactaldehyde dehydrogenase activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0008911 | molecular_function | lactaldehyde dehydrogenase activity |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0008911 | molecular_function | lactaldehyde dehydrogenase activity |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 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 | 17 |
| Details | BINDING SITE FOR RESIDUE NAD A 501 |
| Chain | Residue |
| A | ILE154 |
| A | PHE232 |
| A | SER235 |
| A | VAL238 |
| A | LEU241 |
| A | HOH737 |
| A | HOH765 |
| A | HOH771 |
| A | HOH930 |
| A | THR155 |
| A | PRO156 |
| A | PHE157 |
| A | LYS181 |
| A | THR183 |
| A | GLU184 |
| A | PRO214 |
| A | GLY218 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE POA A 502 |
| Chain | Residue |
| A | ARG108 |
| A | ASN158 |
| A | HIS159 |
| A | MET163 |
| A | GLU254 |
| A | ARG290 |
| A | CYS291 |
| A | THR292 |
| A | ARG447 |
| A | HOH618 |
| A | HOH647 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAD B 501 |
| Chain | Residue |
| B | ILE154 |
| B | THR155 |
| B | PRO156 |
| B | PHE157 |
| B | LYS181 |
| B | THR183 |
| B | GLU184 |
| B | PRO214 |
| B | GLY218 |
| B | PHE232 |
| B | SER235 |
| B | VAL238 |
| B | LEU241 |
| B | HOH641 |
| B | HOH745 |
| B | HOH831 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE POA B 502 |
| Chain | Residue |
| B | ARG108 |
| B | HIS159 |
| B | GLU254 |
| B | ARG290 |
| B | CYS291 |
| B | THR292 |
| B | ARG447 |
| B | HOH604 |
| B | HOH683 |
| B | HOH972 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NAD C 501 |
| Chain | Residue |
| C | ILE154 |
| C | THR155 |
| C | PRO156 |
| C | PHE157 |
| C | LYS181 |
| C | THR183 |
| C | GLU184 |
| C | GLY218 |
| C | PHE232 |
| C | GLY234 |
| C | SER235 |
| C | VAL238 |
| C | LEU241 |
| C | HOH775 |
| C | HOH869 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE POA C 502 |
| Chain | Residue |
| C | ARG108 |
| C | HIS159 |
| C | ARG290 |
| C | CYS291 |
| C | THR292 |
| C | ARG447 |
| C | HOH606 |
| C | HOH698 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAD D 501 |
| Chain | Residue |
| D | ILE154 |
| D | THR155 |
| D | PRO156 |
| D | PHE157 |
| D | LYS181 |
| D | THR183 |
| D | GLU184 |
| D | PRO214 |
| D | GLY218 |
| D | PHE232 |
| D | SER235 |
| D | VAL238 |
| D | LEU241 |
| D | HOH753 |
| D | HOH758 |
| D | HOH907 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE POA D 502 |
| Chain | Residue |
| D | ARG447 |
| D | HOH628 |
| D | HOH679 |
| D | HOH909 |
| D | ARG108 |
| D | ASN158 |
| D | HIS159 |
| D | ARG290 |
| D | CYS291 |
| D | THR292 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NAD E 501 |
| Chain | Residue |
| E | ILE154 |
| E | THR155 |
| E | PRO156 |
| E | PHE157 |
| E | LYS181 |
| E | THR183 |
| E | GLU184 |
| E | GLY218 |
| E | PHE232 |
| E | SER235 |
| E | VAL238 |
| E | HOH776 |
| E | HOH801 |
| E | HOH897 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE POA E 502 |
| Chain | Residue |
| E | ARG108 |
| E | ASN158 |
| E | HIS159 |
| E | ARG290 |
| E | CYS291 |
| E | THR292 |
| E | ARG447 |
| E | HOH620 |
| E | HOH623 |
| E | HOH764 |
| site_id | BC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NAD F 501 |
| Chain | Residue |
| F | ILE154 |
| F | THR155 |
| F | PRO156 |
| F | PHE157 |
| F | LYS181 |
| F | THR183 |
| F | GLU184 |
| F | GLY218 |
| F | PHE232 |
| F | SER235 |
| F | VAL238 |
| F | HOH760 |
| F | HOH770 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE POA F 502 |
| Chain | Residue |
| F | ARG108 |
| F | ASN158 |
| F | HIS159 |
| F | MET163 |
| F | ARG290 |
| F | CYS291 |
| F | THR292 |
| F | ARG447 |
| F | HOH604 |
| site_id | BC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD G 501 |
| Chain | Residue |
| G | ILE154 |
| G | THR155 |
| G | PRO156 |
| G | PHE157 |
| G | LYS181 |
| G | THR183 |
| G | GLU184 |
| G | PRO214 |
| G | GLY218 |
| G | PHE232 |
| G | SER235 |
| G | VAL238 |
| G | LEU241 |
| G | HOH637 |
| G | HOH722 |
| G | HOH818 |
| G | HOH849 |
| G | HOH907 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE POA G 502 |
| Chain | Residue |
| G | ARG108 |
| G | ASN158 |
| G | HIS159 |
| G | MET163 |
| G | ARG290 |
| G | CYS291 |
| G | THR292 |
| G | ARG447 |
| G | HOH606 |
| G | HOH610 |
| site_id | BC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE POA H 501 |
| Chain | Residue |
| H | ARG108 |
| H | ASN158 |
| H | HIS159 |
| H | GLU254 |
| H | ARG290 |
| H | CYS291 |
| H | THR292 |
| H | ARG447 |
| H | HOH722 |
| H | HOH819 |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGNDP |
| Chain | Residue | Details |
| A | LEU253-PRO260 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000269|PubMed:24361046 |
| Chain | Residue | Details |
| A | GLU254 | |
| B | GLU254 | |
| C | GLU254 | |
| D | GLU254 | |
| E | GLU254 | |
| F | GLU254 | |
| G | GLU254 | |
| H | GLU254 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:24361046 |
| Chain | Residue | Details |
| F | CYS291 | |
| A | CYS291 | |
| B | CYS291 | |
| C | CYS291 | |
| D | CYS291 | |
| E | CYS291 | |
| G | CYS291 | |
| H | CYS291 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24361046, ECO:0007744|PDB:4I3X |
| Chain | Residue | Details |
| B | GLU385 | |
| B | ARG447 | |
| C | ARG108 | |
| C | HIS159 | |
| C | ARG290 | |
| C | GLU385 | |
| C | ARG447 | |
| D | ARG108 | |
| D | HIS159 | |
| D | ARG290 | |
| D | GLU385 | |
| D | ARG447 | |
| E | ARG108 | |
| E | HIS159 | |
| E | ARG290 | |
| E | GLU385 | |
| E | ARG447 | |
| F | ARG108 | |
| F | HIS159 | |
| F | ARG290 | |
| F | GLU385 | |
| F | ARG447 | |
| G | ARG108 | |
| G | HIS159 | |
| G | ARG290 | |
| G | GLU385 | |
| G | ARG447 | |
| H | ARG108 | |
| H | HIS159 | |
| H | ARG290 | |
| H | GLU385 | |
| H | ARG447 | |
| A | ARG108 | |
| A | HIS159 | |
| A | ARG290 | |
| A | GLU385 | |
| A | ARG447 | |
| B | ARG108 | |
| B | HIS159 | |
| B | ARG290 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24361046, ECO:0007744|PDB:4I3V, ECO:0007744|PDB:4I3W, ECO:0007744|PDB:4I3X |
| Chain | Residue | Details |
| E | THR155 | |
| E | LYS181 | |
| E | SER235 | |
| F | THR155 | |
| F | LYS181 | |
| F | SER235 | |
| A | THR155 | |
| A | LYS181 | |
| A | SER235 | |
| B | THR155 | |
| B | LYS181 | |
| B | SER235 | |
| C | THR155 | |
| C | LYS181 | |
| C | SER235 | |
| D | THR155 | |
| D | LYS181 | |
| D | SER235 | |
| G | THR155 | |
| G | LYS181 | |
| G | SER235 | |
| H | THR155 | |
| H | LYS181 | |
| H | SER235 |
