1EUH
APO FORM OF A NADP DEPENDENT ALDEHYDE DEHYDROGENASE FROM STREPTOCOCCUS MUTANS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) 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 | 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 | 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 | 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 A 476 |
| Chain | Residue |
| A | ARG103 |
| A | ARG283 |
| A | GLN436 |
| A | ARG437 |
| A | GLY438 |
| A | HOH736 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 477 |
| Chain | Residue |
| A | HOH635 |
| A | HOH797 |
| A | HOH806 |
| A | THR180 |
| A | GLY210 |
| A | HOH626 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 476 |
| Chain | Residue |
| B | ARG103 |
| B | GLN436 |
| B | ARG437 |
| B | GLY438 |
| B | HOH638 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 477 |
| Chain | Residue |
| B | THR180 |
| B | GLY208 |
| B | ARG209 |
| B | GLY210 |
| B | HOH633 |
| B | HOH769 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 478 |
| Chain | Residue |
| B | ASP327 |
| B | THR328 |
| B | LYS329 |
| B | HOH604 |
| B | HOH782 |
| C | GLU351 |
| C | HOH599 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 476 |
| Chain | Residue |
| C | ARG103 |
| C | ARG283 |
| C | GLN436 |
| C | ARG437 |
| C | GLY438 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 477 |
| Chain | Residue |
| C | THR180 |
| C | GLY208 |
| C | ARG209 |
| C | GLY210 |
| C | HOH565 |
| C | HOH603 |
| C | HOH776 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 476 |
| Chain | Residue |
| D | ARG103 |
| D | GLN436 |
| D | ARG437 |
| D | GLY438 |
| D | HOH674 |
| D | HOH691 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 477 |
| Chain | Residue |
| D | THR180 |
| D | ARG209 |
| D | GLY210 |
| D | HOH580 |
| D | HOH683 |
| D | HOH700 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 478 |
| Chain | Residue |
| A | GLU351 |
| A | HOH759 |
| D | ASP327 |
| D | THR328 |
| D | LYS329 |
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 | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| A | ASN154 | |
| A | CYS284 | |
| A | GLU250 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| B | ASN154 | |
| B | CYS284 | |
| B | GLU250 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| C | ASN154 | |
| C | CYS284 | |
| C | GLU250 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| D | ASN154 | |
| D | CYS284 | |
| 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 | 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 |
