1QI1
Ternary Complex of an NADP Dependent Aldehyde Dehydrogenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
| 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 |
| A | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
| B | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
| 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 |
| B | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
| C | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
| 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 |
| C | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
| D | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
| 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 |
| D | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAP A 500 |
| Chain | Residue |
| A | ILE150 |
| A | GLY210 |
| A | GLY214 |
| A | ASP215 |
| A | PHE228 |
| A | THR229 |
| A | GLY230 |
| A | SER231 |
| A | ILE234 |
| A | GLU250 |
| A | LEU251 |
| A | SER151 |
| A | SER284 |
| A | PHE379 |
| A | G3H504 |
| A | PRO152 |
| A | PHE153 |
| A | ASN154 |
| A | LEU159 |
| A | LYS177 |
| A | PRO179 |
| A | THR180 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAP B 501 |
| Chain | Residue |
| B | ILE150 |
| B | SER151 |
| B | PRO152 |
| B | PHE153 |
| B | ASN154 |
| B | TYR155 |
| B | LEU159 |
| B | LYS177 |
| B | PRO179 |
| B | THR180 |
| B | GLY208 |
| B | GLY210 |
| B | GLY214 |
| B | ASP215 |
| B | PHE228 |
| B | GLY230 |
| B | SER231 |
| B | ILE234 |
| B | GLU250 |
| B | LEU251 |
| B | SER284 |
| B | G3P505 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAP C 502 |
| Chain | Residue |
| C | ILE150 |
| C | SER151 |
| C | PHE153 |
| C | ASN154 |
| C | TYR155 |
| C | LEU159 |
| C | LYS177 |
| C | PRO178 |
| C | PRO179 |
| C | THR180 |
| C | GLY210 |
| C | GLY214 |
| C | ASP215 |
| C | PHE228 |
| C | THR229 |
| C | GLY230 |
| C | SER231 |
| C | ILE234 |
| C | GLU250 |
| C | LEU251 |
| C | SER284 |
| C | GLU377 |
| C | PHE379 |
| C | G3H506 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAP D 503 |
| Chain | Residue |
| D | ILE150 |
| D | SER151 |
| D | PRO152 |
| D | PHE153 |
| D | ASN154 |
| D | LEU159 |
| D | LYS177 |
| D | PRO179 |
| D | THR180 |
| D | GLY214 |
| D | ASP215 |
| D | VAL218 |
| D | PHE228 |
| D | GLY230 |
| D | SER231 |
| D | ILE234 |
| D | GLU250 |
| D | LEU251 |
| D | GLY252 |
| D | SER284 |
| D | GLU377 |
| D | PHE379 |
| D | G3H507 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE G3H A 504 |
| Chain | Residue |
| A | NAP500 |
| A | ARG103 |
| A | ASN154 |
| A | TYR155 |
| A | ARG283 |
| A | SER284 |
| A | THR285 |
| A | GLN436 |
| A | ARG437 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE G3P B 505 |
| Chain | Residue |
| B | ARG103 |
| B | TYR155 |
| B | GLU250 |
| B | ARG283 |
| B | SER284 |
| B | THR285 |
| B | GLN436 |
| B | ARG437 |
| B | NAP501 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE G3H C 506 |
| Chain | Residue |
| C | ARG103 |
| C | ASN154 |
| C | TYR155 |
| C | ARG283 |
| C | SER284 |
| C | THR285 |
| C | GLN436 |
| C | ARG437 |
| C | NAP502 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE G3H D 507 |
| Chain | Residue |
| D | ARG103 |
| D | TYR155 |
| D | ARG283 |
| D | SER284 |
| D | THR285 |
| D | GLN436 |
| D | ARG437 |
| D | NAP503 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10864505","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 104 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10388564","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10864505","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16958622","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1o04 |
| Chain | Residue | Details |
| A | LYS177 | |
| A | GLU377 | |
| A | SER284 | |
| A | GLU250 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1o04 |
| Chain | Residue | Details |
| B | LYS177 | |
| B | GLU377 | |
| B | SER284 | |
| B | GLU250 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1o04 |
| Chain | Residue | Details |
| C | LYS177 | |
| C | GLU377 | |
| C | SER284 | |
| C | GLU250 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1o04 |
| Chain | Residue | Details |
| D | LYS177 | |
| D | GLU377 | |
| D | SER284 | |
| D | GLU250 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 711 |
| Chain | Residue | Details |
| A | ASN154 | electrostatic stabiliser |
| A | GLU250 | activator, electrostatic stabiliser, proton acceptor, proton donor |
| A | SER284 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 711 |
| Chain | Residue | Details |
| B | ASN154 | electrostatic stabiliser |
| B | GLU250 | activator, electrostatic stabiliser, proton acceptor, proton donor |
| B | SER284 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 711 |
| Chain | Residue | Details |
| C | ASN154 | electrostatic stabiliser |
| C | GLU250 | activator, electrostatic stabiliser, proton acceptor, proton donor |
| C | SER284 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 711 |
| Chain | Residue | Details |
| D | ASN154 | electrostatic stabiliser |
| D | GLU250 | activator, electrostatic stabiliser, proton acceptor, proton donor |
| D | SER284 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor |
