6FZI
Crystal Structure of a Clostridial Dehydrogenase at 2.55 Angstroems Resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006006 | biological_process | glucose metabolic process |
| 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 | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006006 | biological_process | glucose metabolic process |
| 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 | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006006 | biological_process | glucose metabolic process |
| 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 | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006006 | biological_process | glucose metabolic process |
| 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 | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue NAD A 401 |
| Chain | Residue |
| A | GLY8 |
| A | CYS95 |
| A | THR96 |
| A | GLY97 |
| A | PHE98 |
| A | PHE99 |
| A | SER119 |
| A | ALA120 |
| A | CYS150 |
| A | ASN181 |
| A | ASN314 |
| A | GLY10 |
| A | TYR318 |
| A | PEG406 |
| A | ACT407 |
| A | HOH503 |
| B | PRO189 |
| A | ARG11 |
| A | ILE12 |
| A | ASN32 |
| A | ASP33 |
| A | LEU34 |
| A | LYS76 |
| A | SER77 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | ARG196 |
| A | ASN208 |
| A | SER209 |
| C | THR293 |
| C | LYS296 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | ALA202 |
| C | ALA202 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | LEU248 |
| A | ASP249 |
| A | GLY302 |
| A | GLN303 |
| A | GLN304 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | HIS42 |
| A | LYS45 |
| A | ILE57 |
| D | ASP274 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 406 |
| Chain | Residue |
| A | THR180 |
| A | ASP182 |
| A | ARG233 |
| A | NAD401 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue ACT A 407 |
| Chain | Residue |
| A | PHE98 |
| A | NAD401 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | binding site for residue NAD B 401 |
| Chain | Residue |
| B | GLY8 |
| B | GLY10 |
| B | ARG11 |
| B | ILE12 |
| B | ASN32 |
| B | ASP33 |
| B | LEU34 |
| B | LYS76 |
| B | SER77 |
| B | CYS95 |
| B | GLY97 |
| B | PHE98 |
| B | PHE99 |
| B | SER119 |
| B | ALA120 |
| B | ASN181 |
| B | ASN314 |
| B | TYR318 |
| B | PEG404 |
| B | HOH509 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | ARG196 |
| B | ASN208 |
| B | SER209 |
| B | ASN230 |
| B | GOL403 |
| D | THR293 |
| D | LYS296 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | GLY193 |
| B | ASP194 |
| B | LEU195 |
| B | GOL402 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 404 |
| Chain | Residue |
| B | CYS150 |
| B | THR180 |
| B | ASP182 |
| B | NAD401 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue ACT B 405 |
| Chain | Residue |
| B | LEU248 |
| B | GLY302 |
| B | GLN304 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue ACT B 406 |
| Chain | Residue |
| B | HIS42 |
| C | ASP274 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue ACT B 407 |
| Chain | Residue |
| B | VAL133 |
| B | HIS135 |
| B | ASP136 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue ACT B 408 |
| Chain | Residue |
| B | ILE284 |
| B | SER285 |
| C | ARG52 |
| site_id | AD7 |
| Number of Residues | 18 |
| Details | binding site for residue NAD C 401 |
| Chain | Residue |
| C | SER77 |
| C | CYS95 |
| C | GLY97 |
| C | PHE98 |
| C | PHE99 |
| C | SER119 |
| C | ALA120 |
| C | CYS150 |
| C | ASN314 |
| C | TYR318 |
| D | PRO189 |
| C | GLY10 |
| C | ARG11 |
| C | ILE12 |
| C | ASN32 |
| C | ASP33 |
| C | LEU34 |
| C | LYS76 |
| site_id | AD8 |
| Number of Residues | 1 |
| Details | binding site for residue GOL C 402 |
| Chain | Residue |
| C | ASN165 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL C 403 |
| Chain | Residue |
| C | GLU267 |
| C | ASN320 |
| C | ILE323 |
| C | ARG324 |
| C | LYS327 |
| site_id | AE1 |
| Number of Residues | 1 |
| Details | binding site for residue GOL C 404 |
| Chain | Residue |
| C | ASP164 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 405 |
| Chain | Residue |
| C | ARG196 |
| C | PRO207 |
| C | ASN208 |
| C | SER209 |
| site_id | AE3 |
| Number of Residues | 20 |
| Details | binding site for residue NAD D 401 |
| Chain | Residue |
| C | PRO189 |
| D | GLY8 |
| D | GLY10 |
| D | ARG11 |
| D | ILE12 |
| D | ASN32 |
| D | ASP33 |
| D | LYS76 |
| D | SER77 |
| D | CYS95 |
| D | THR96 |
| D | GLY97 |
| D | PHE98 |
| D | PHE99 |
| D | SER119 |
| D | ALA120 |
| D | CYS150 |
| D | ASN181 |
| D | ASN314 |
| D | TYR318 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 402 |
| Chain | Residue |
| B | THR293 |
| B | LYS296 |
| D | ARG196 |
| D | ASN208 |
| D | SER209 |
| D | ACT404 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue ACT D 403 |
| Chain | Residue |
| D | VAL133 |
| D | ASN134 |
| D | HIS135 |
| D | ASP136 |
| site_id | AE6 |
| Number of Residues | 4 |
| Details | binding site for residue ACT D 404 |
| Chain | Residue |
| B | PRO275 |
| D | ASP194 |
| D | LEU195 |
| D | GOL402 |
| site_id | AE7 |
| Number of Residues | 4 |
| Details | binding site for residue ACT D 405 |
| Chain | Residue |
| D | ASN23 |
| D | GLU267 |
| D | ASN320 |
| D | LYS327 |
Functional Information from PROSITE/UniProt
| site_id | PS00071 |
| Number of Residues | 8 |
| Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
| Chain | Residue | Details |
| A | ALA148-LEU155 |
