4I3X
Structure of phosphonoacetaldehyde dehydrogenase in complex with phosphonoacetate 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 | 30 |
| Details | BINDING SITE FOR RESIDUE NAD A 501 |
| Chain | Residue |
| A | ILE154 |
| A | GLY218 |
| A | PHE232 |
| A | THR233 |
| A | GLY234 |
| A | SER235 |
| A | VAL238 |
| A | GLU254 |
| A | LEU255 |
| A | GLY256 |
| A | GLY257 |
| A | THR155 |
| A | CYS291 |
| A | GLU385 |
| A | PHE387 |
| A | PHE453 |
| A | PAE502 |
| A | HOH686 |
| A | HOH720 |
| A | HOH834 |
| A | HOH935 |
| A | HOH947 |
| A | PRO156 |
| A | HOH1004 |
| A | PHE157 |
| A | ASN158 |
| A | LYS181 |
| A | THR183 |
| A | GLU184 |
| A | PRO214 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PAE A 502 |
| Chain | Residue |
| A | ARG108 |
| A | ASN158 |
| A | HIS159 |
| A | ARG290 |
| A | CYS291 |
| A | THR292 |
| A | ARG447 |
| A | NAD501 |
| A | HOH627 |
| A | HOH719 |
| A | HOH723 |
| A | HOH1070 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD B 501 |
| Chain | Residue |
| B | ILE154 |
| B | THR155 |
| B | PRO156 |
| B | PHE157 |
| B | ASN158 |
| B | LYS181 |
| B | THR183 |
| B | GLU184 |
| B | PRO214 |
| B | GLY218 |
| B | PHE232 |
| B | THR233 |
| B | GLY234 |
| B | SER235 |
| B | VAL238 |
| B | GLU254 |
| B | LEU255 |
| B | GLY256 |
| B | GLY257 |
| B | CYS291 |
| B | GLU385 |
| B | PHE387 |
| B | PHE453 |
| B | PAE502 |
| B | HOH632 |
| B | HOH676 |
| B | HOH843 |
| B | HOH899 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PAE B 502 |
| Chain | Residue |
| B | ARG108 |
| B | ASN158 |
| B | HIS159 |
| B | ARG290 |
| B | CYS291 |
| B | ARG447 |
| B | NAD501 |
| B | HOH621 |
| B | HOH648 |
| B | HOH961 |
| B | HOH978 |
| site_id | AC5 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD C 501 |
| Chain | Residue |
| C | GLY257 |
| C | CYS291 |
| C | GLU385 |
| C | PHE387 |
| C | PHE453 |
| C | PAE502 |
| C | HOH642 |
| C | HOH702 |
| C | HOH713 |
| C | HOH770 |
| C | HOH779 |
| C | HOH929 |
| C | ILE154 |
| C | THR155 |
| C | PRO156 |
| C | PHE157 |
| C | ASN158 |
| C | LYS181 |
| C | THR183 |
| C | GLU184 |
| C | PRO214 |
| C | GLY218 |
| C | PHE232 |
| C | THR233 |
| C | GLY234 |
| C | SER235 |
| C | VAL238 |
| C | GLU254 |
| C | LEU255 |
| C | GLY256 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PAE C 502 |
| Chain | Residue |
| C | ARG108 |
| C | ASN158 |
| C | HIS159 |
| C | ARG290 |
| C | CYS291 |
| C | THR292 |
| C | ARG447 |
| C | NAD501 |
| C | HOH606 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD D 501 |
| Chain | Residue |
| D | ILE154 |
| D | THR155 |
| D | PRO156 |
| D | PHE157 |
| D | ASN158 |
| D | LYS181 |
| D | THR183 |
| D | GLU184 |
| D | PRO214 |
| D | GLY218 |
| D | PHE232 |
| D | THR233 |
| D | GLY234 |
| D | SER235 |
| D | VAL238 |
| D | LEU241 |
| D | GLU254 |
| D | LEU255 |
| D | GLY256 |
| D | GLY257 |
| D | CYS291 |
| D | GLU385 |
| D | PHE387 |
| D | PHE453 |
| D | PAE502 |
| D | HOH645 |
| D | HOH700 |
| D | HOH807 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PAE D 502 |
| Chain | Residue |
| D | ARG108 |
| D | ASN158 |
| D | HIS159 |
| D | ARG290 |
| D | CYS291 |
| D | ARG447 |
| D | NAD501 |
| D | HOH624 |
| D | HOH719 |
| site_id | AC9 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD E 501 |
| Chain | Residue |
| E | ILE154 |
| E | THR155 |
| E | PRO156 |
| E | PHE157 |
| E | ASN158 |
| E | LYS181 |
| E | THR183 |
| E | GLU184 |
| E | GLY218 |
| E | PHE232 |
| E | THR233 |
| E | GLY234 |
| E | SER235 |
| E | VAL238 |
| E | LEU241 |
| E | GLU254 |
| E | LEU255 |
| E | GLY256 |
| E | GLY257 |
| E | CYS291 |
| E | GLU385 |
| E | PHE387 |
| E | PHE453 |
| E | PAE502 |
| E | HOH644 |
| E | HOH691 |
| E | HOH765 |
| E | HOH783 |
| E | HOH793 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PAE E 502 |
| Chain | Residue |
| E | ARG108 |
| E | ASN158 |
| E | HIS159 |
| E | ARG290 |
| E | CYS291 |
| E | THR292 |
| E | ARG447 |
| E | NAD501 |
| E | HOH628 |
| E | HOH679 |
| site_id | BC2 |
| Number of Residues | 27 |
| 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 | THR233 |
| F | GLY234 |
| F | SER235 |
| F | VAL238 |
| F | LEU241 |
| F | GLU254 |
| F | LEU255 |
| F | GLY256 |
| F | GLY257 |
| F | CYS291 |
| F | GLU385 |
| F | PHE387 |
| F | PHE453 |
| F | PAE502 |
| F | HOH617 |
| F | HOH724 |
| F | HOH821 |
| F | HOH826 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PAE F 502 |
| Chain | Residue |
| F | ARG108 |
| F | ASN158 |
| F | HIS159 |
| F | ARG290 |
| F | CYS291 |
| F | THR292 |
| F | ARG447 |
| F | NAD501 |
| F | HOH675 |
| F | HOH758 |
| F | HOH775 |
| site_id | BC4 |
| Number of Residues | 28 |
| 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 | THR233 |
| G | GLY234 |
| G | SER235 |
| G | VAL238 |
| G | LEU241 |
| G | GLU254 |
| G | LEU255 |
| G | GLY256 |
| G | GLY257 |
| G | CYS291 |
| G | GLU385 |
| G | PHE387 |
| G | PHE453 |
| G | PAE502 |
| G | HOH695 |
| G | HOH844 |
| G | HOH897 |
| G | HOH932 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PAE G 502 |
| Chain | Residue |
| G | ARG108 |
| G | HIS159 |
| G | ARG290 |
| G | CYS291 |
| G | THR292 |
| G | ARG447 |
| G | NAD501 |
| G | HOH624 |
| G | HOH696 |
| G | HOH760 |
| site_id | BC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD H 501 |
| Chain | Residue |
| H | ILE154 |
| H | THR155 |
| H | PRO156 |
| H | PHE157 |
| H | ASN158 |
| H | LYS181 |
| H | THR183 |
| H | GLU184 |
| H | GLY218 |
| H | PHE232 |
| H | THR233 |
| H | GLY234 |
| H | SER235 |
| H | VAL238 |
| H | LEU241 |
| H | GLU254 |
| H | LEU255 |
| H | GLY256 |
| H | GLY257 |
| H | CYS291 |
| H | GLU385 |
| H | PHE387 |
| H | PHE453 |
| H | PAE502 |
| H | HOH669 |
| H | HOH716 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PAE H 502 |
| Chain | Residue |
| H | ARG108 |
| H | ASN158 |
| H | HIS159 |
| H | ARG290 |
| H | CYS291 |
| H | ARG447 |
| H | NAD501 |
| H | HOH668 |
| H | HOH833 |
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 |
| A | CYS291 | |
| C | CYS291 | |
| D | CYS291 | |
| E | CYS291 | |
| F | CYS291 | |
| G | CYS291 | |
| H | CYS291 | |
| B | 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 |
| H | 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 | |
| E | THR155 | |
| E | LYS181 | |
| E | SER235 | |
| F | THR155 | |
| F | LYS181 | |
| F | SER235 | |
| G | THR155 | |
| G | LYS181 | |
| G | SER235 | |
| H | THR155 | |
| H | LYS181 |
