4I3W
Structure of phosphonoacetaldehyde dehydrogenase in complex with gylceraldehyde-3-phosphate and cofactor NAD+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) 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 (NAD+) 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 (NAD+) 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 (NAD+) 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 (NAD+) 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 (NAD+) 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 (NAD+) 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 (NAD+) 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 | 10 |
| Details | BINDING SITE FOR RESIDUE G3H A 501 |
| Chain | Residue |
| A | ARG108 |
| A | HOH850 |
| A | ASN158 |
| A | HIS159 |
| A | ARG290 |
| A | CYS291 |
| A | THR292 |
| A | ARG447 |
| A | PHE453 |
| A | HOH614 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAD A 502 |
| Chain | Residue |
| A | ILE154 |
| A | THR155 |
| A | PRO156 |
| A | PHE157 |
| A | LYS181 |
| A | THR183 |
| A | GLU184 |
| A | PRO214 |
| A | GLY218 |
| A | PHE232 |
| A | GLY234 |
| A | SER235 |
| A | VAL238 |
| A | LEU241 |
| A | HOH652 |
| A | HOH798 |
| A | HOH854 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE G3H B 501 |
| Chain | Residue |
| B | ARG108 |
| B | ASN158 |
| B | HIS159 |
| B | THR233 |
| B | ARG290 |
| B | CYS291 |
| B | THR292 |
| B | ARG447 |
| B | PHE453 |
| B | HOH617 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NAD B 502 |
| 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 | HOH745 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE G3H C 501 |
| Chain | Residue |
| C | ARG108 |
| C | ASN158 |
| C | HIS159 |
| C | THR233 |
| C | ARG290 |
| C | CYS291 |
| C | ARG447 |
| C | HOH651 |
| C | HOH707 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NAD C 502 |
| Chain | Residue |
| C | ILE154 |
| C | THR155 |
| C | PRO156 |
| C | PHE157 |
| C | LYS181 |
| C | THR183 |
| C | GLU184 |
| C | PRO214 |
| C | PHE232 |
| C | THR233 |
| C | SER235 |
| C | VAL238 |
| C | LEU241 |
| C | HIS335 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE G3H D 501 |
| Chain | Residue |
| D | ARG108 |
| D | ASN158 |
| D | HIS159 |
| D | THR233 |
| D | ARG290 |
| D | CYS291 |
| D | ARG447 |
| D | HOH622 |
| D | HOH632 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NAD D 502 |
| 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 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE G3H E 501 |
| Chain | Residue |
| E | ARG290 |
| E | CYS291 |
| E | THR292 |
| E | ARG447 |
| E | HOH653 |
| E | HOH733 |
| E | HOH785 |
| E | ARG108 |
| E | ASN158 |
| E | HIS159 |
| E | THR233 |
| site_id | BC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAD E 502 |
| Chain | Residue |
| E | ILE154 |
| E | THR155 |
| E | PRO156 |
| E | PHE157 |
| E | LYS181 |
| E | THR183 |
| E | GLU184 |
| E | PRO214 |
| E | GLY218 |
| E | PHE232 |
| E | GLY234 |
| E | SER235 |
| E | VAL238 |
| E | LEU241 |
| E | HOH635 |
| E | HOH786 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE G3H F 501 |
| Chain | Residue |
| F | ARG108 |
| F | ASN158 |
| F | HIS159 |
| F | THR233 |
| F | ARG290 |
| F | CYS291 |
| F | ARG447 |
| F | HOH604 |
| F | HOH631 |
| F | HOH664 |
| F | HOH720 |
| site_id | BC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAD F 502 |
| Chain | Residue |
| F | ILE154 |
| F | THR155 |
| F | PRO156 |
| F | PHE157 |
| F | LYS181 |
| F | PRO182 |
| F | THR183 |
| F | GLU184 |
| F | PRO214 |
| F | GLY218 |
| F | PHE232 |
| F | GLY234 |
| F | SER235 |
| F | VAL238 |
| F | LEU241 |
| F | HOH684 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE G3H G 501 |
| Chain | Residue |
| G | ARG108 |
| G | ASN158 |
| G | HIS159 |
| G | THR233 |
| G | ARG290 |
| G | CYS291 |
| G | THR292 |
| G | ARG447 |
| G | HOH742 |
| site_id | BC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NAD G 502 |
| Chain | Residue |
| G | ILE154 |
| G | THR155 |
| G | PRO156 |
| G | PHE157 |
| G | LYS181 |
| G | PRO182 |
| G | THR183 |
| G | GLU184 |
| G | PRO214 |
| G | GLY218 |
| G | PHE232 |
| G | SER235 |
| G | VAL238 |
| G | LEU241 |
| G | HOH616 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE G3H H 501 |
| Chain | Residue |
| H | ARG108 |
| H | ASN158 |
| H | HIS159 |
| H | ARG290 |
| H | CYS291 |
| H | ARG447 |
| H | PHE453 |
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 | |
| B | CYS291 | |
| C | CYS291 | |
| D | CYS291 | |
| E | CYS291 | |
| F | 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 |
| A | ARG108 | |
| B | ARG447 | |
| C | ARG108 | |
| C | HIS159 | |
| C | ARG290 | |
| C | GLU385 | |
| C | ARG447 | |
| D | ARG108 | |
| D | HIS159 | |
| D | ARG290 | |
| D | GLU385 | |
| A | HIS159 | |
| D | ARG447 | |
| E | ARG108 | |
| E | HIS159 | |
| E | ARG290 | |
| E | GLU385 | |
| E | ARG447 | |
| F | ARG108 | |
| F | HIS159 | |
| F | ARG290 | |
| F | GLU385 | |
| A | ARG290 | |
| F | ARG447 | |
| G | ARG108 | |
| G | HIS159 | |
| G | ARG290 | |
| G | GLU385 | |
| G | ARG447 | |
| H | ARG108 | |
| H | HIS159 | |
| H | ARG290 | |
| H | GLU385 | |
| A | GLU385 | |
| H | ARG447 | |
| A | ARG447 | |
| B | ARG108 | |
| B | HIS159 | |
| B | ARG290 | |
| B | GLU385 |
| 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 |
| A | THR155 | |
| D | THR155 | |
| D | LYS181 | |
| D | SER235 | |
| E | THR155 | |
| E | LYS181 | |
| E | SER235 | |
| F | THR155 | |
| F | LYS181 | |
| F | SER235 | |
| G | THR155 | |
| A | LYS181 | |
| G | LYS181 | |
| G | SER235 | |
| H | THR155 | |
| H | LYS181 | |
| H | SER235 | |
| A | SER235 | |
| B | THR155 | |
| B | LYS181 | |
| B | SER235 | |
| C | THR155 | |
| C | LYS181 | |
| C | SER235 |
