2EUH
HOLO FORM OF A NADP DEPENDENT ALDEHYDE DEHYDROGENASE COMPLEX WITH NADP+
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 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 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 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 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 | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 477 |
| Chain | Residue |
| B | ARG103 |
| B | ARG283 |
| B | THR285 |
| B | GLN436 |
| B | ARG437 |
| B | GLY438 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 478 |
| Chain | Residue |
| C | GLU351 |
| B | ASP327 |
| B | THR328 |
| B | LYS329 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 477 |
| Chain | Residue |
| C | ARG103 |
| C | ARG283 |
| C | THR285 |
| C | GLN436 |
| C | ARG437 |
| C | GLY438 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 477 |
| Chain | Residue |
| D | ARG103 |
| D | ARG283 |
| D | THR285 |
| D | GLN436 |
| D | ARG437 |
| D | GLY438 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 478 |
| Chain | Residue |
| A | GLU351 |
| D | ASP327 |
| D | THR328 |
| D | LYS329 |
| site_id | AC6 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAP A 476 |
| Chain | Residue |
| A | ILE150 |
| A | SER151 |
| A | PRO152 |
| A | PHE153 |
| A | ASN154 |
| A | LYS177 |
| A | PRO179 |
| A | THR180 |
| A | GLY208 |
| A | ARG209 |
| A | GLY210 |
| A | GLY214 |
| A | ASP215 |
| A | VAL218 |
| A | PHE228 |
| A | THR229 |
| A | GLY230 |
| A | SER231 |
| A | ILE234 |
| A | GLU250 |
| A | LEU251 |
| A | GLY252 |
| A | CYS284 |
| A | GLU377 |
| A | PHE379 |
| A | ARG437 |
| A | PHE444 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAP B 476 |
| Chain | Residue |
| B | ILE150 |
| B | SER151 |
| B | PRO152 |
| B | PHE153 |
| B | ASN154 |
| B | LYS177 |
| B | PRO178 |
| B | PRO179 |
| B | THR180 |
| B | GLY210 |
| B | GLY214 |
| B | ASP215 |
| B | PHE228 |
| B | THR229 |
| B | GLY230 |
| B | SER231 |
| B | ILE234 |
| B | GLU250 |
| B | LEU251 |
| B | GLY252 |
| B | CYS284 |
| B | GLU377 |
| B | PHE379 |
| B | ARG437 |
| B | PHE444 |
| B | HOH522 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAP C 476 |
| Chain | Residue |
| C | LEU251 |
| C | CYS284 |
| C | GLU377 |
| C | PHE379 |
| C | LEU405 |
| C | ARG437 |
| C | PHE444 |
| C | HOH526 |
| C | ILE150 |
| C | SER151 |
| C | PRO152 |
| C | PHE153 |
| C | ASN154 |
| C | LEU159 |
| C | LYS177 |
| C | PRO178 |
| C | PRO179 |
| C | THR180 |
| C | ARG209 |
| C | GLY210 |
| C | GLY214 |
| C | ASP215 |
| C | PHE228 |
| C | THR229 |
| C | GLY230 |
| C | SER231 |
| C | ILE234 |
| C | GLU250 |
| site_id | AC9 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAP D 476 |
| Chain | Residue |
| D | ILE150 |
| D | SER151 |
| D | PRO152 |
| D | PHE153 |
| D | ASN154 |
| D | LEU159 |
| D | LYS177 |
| D | PRO178 |
| D | PRO179 |
| D | THR180 |
| D | GLY208 |
| D | ARG209 |
| D | GLY210 |
| D | GLY214 |
| D | ASP215 |
| D | VAL218 |
| D | PHE228 |
| D | THR229 |
| D | GLY230 |
| D | SER231 |
| D | ILE234 |
| D | GLU250 |
| D | LEU251 |
| D | GLY252 |
| D | CYS284 |
| D | GLU377 |
| D | PHE379 |
| D | LEU405 |
| D | ARG437 |
| D | PHE444 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FgYSGQRCTAVK |
| Chain | Residue | Details |
| A | PHE277-LYS288 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10008 |
| Chain | Residue | Details |
| A | GLU250 | |
| A | CYS284 | |
| B | GLU250 | |
| B | CYS284 | |
| C | GLU250 | |
| C | CYS284 | |
| D | GLU250 | |
| D | CYS284 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10864505 |
| Chain | Residue | Details |
| A | ARG103 | |
| A | ARG437 | |
| B | ARG103 | |
| B | ARG437 | |
| C | ARG103 | |
| C | ARG437 | |
| D | ARG103 | |
| D | ARG437 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10388564, ECO:0000269|PubMed:10864505, ECO:0000269|PubMed:16958622 |
| Chain | Residue | Details |
| A | SER151 | |
| B | ASP215 | |
| B | GLY230 | |
| B | GLU377 | |
| C | SER151 | |
| C | LYS177 | |
| C | THR180 | |
| C | ASP215 | |
| C | GLY230 | |
| C | GLU377 | |
| D | SER151 | |
| A | LYS177 | |
| D | LYS177 | |
| D | THR180 | |
| D | ASP215 | |
| D | GLY230 | |
| D | GLU377 | |
| A | THR180 | |
| A | ASP215 | |
| A | GLY230 | |
| A | GLU377 | |
| B | SER151 | |
| B | LYS177 | |
| B | THR180 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN154 | |
| A | ARG283 | |
| B | ASN154 | |
| B | ARG283 | |
| C | ASN154 | |
| C | ARG283 | |
| D | ASN154 | |
| D | ARG283 |
Catalytic Information from CSA
| 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 | CYS284 | 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 | CYS284 | 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 | CYS284 | 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 | CYS284 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor |
