7C5K
Crystal Structure of C150S mutant of Glyceraldehyde-3-phosphate-dehydrogenase1 from Escherichia coli complexed with G3P at 2.69 Angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| O | 0006006 | biological_process | glucose metabolic process |
| O | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| O | 0050661 | molecular_function | NADP binding |
| O | 0051287 | molecular_function | NAD binding |
| P | 0006006 | biological_process | glucose metabolic process |
| P | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| P | 0050661 | molecular_function | NADP binding |
| P | 0051287 | molecular_function | NAD binding |
| Q | 0006006 | biological_process | glucose metabolic process |
| Q | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| Q | 0050661 | molecular_function | NADP binding |
| Q | 0051287 | molecular_function | NAD binding |
| R | 0006006 | biological_process | glucose metabolic process |
| R | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| R | 0050661 | molecular_function | NADP binding |
| R | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue NAD O 401 |
| Chain | Residue |
| O | ASN7 |
| O | LYS78 |
| O | CYS96 |
| O | THR97 |
| O | GLY98 |
| O | PHE99 |
| O | SER120 |
| O | ALA121 |
| O | SER150 |
| O | THR180 |
| O | ASN315 |
| O | GLY8 |
| O | PHE319 |
| O | G3H402 |
| O | HOH513 |
| O | HOH533 |
| O | HOH537 |
| O | HOH543 |
| O | HOH559 |
| O | HOH588 |
| O | HOH615 |
| O | PHE9 |
| O | GLY10 |
| O | ARG11 |
| O | ILE12 |
| O | ASN33 |
| O | ASP34 |
| O | LEU35 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue G3H O 402 |
| Chain | Residue |
| O | SER149 |
| O | SER150 |
| O | THR151 |
| O | HIS177 |
| O | THR180 |
| O | THR182 |
| O | THR209 |
| O | ARG232 |
| O | NAD401 |
| O | HOH609 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 O 403 |
| Chain | Residue |
| O | HIS163 |
| O | GLY167 |
| O | ILE168 |
| O | GLU169 |
| O | LYS225 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue PO4 O 404 |
| Chain | Residue |
| O | ALA201 |
| O | GLU202 |
| O | HOH562 |
| P | ALA201 |
| P | HOH556 |
| P | HOH567 |
| P | HOH574 |
| Q | ALA201 |
| R | ALA201 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | binding site for residue NAD P 401 |
| Chain | Residue |
| P | ASN7 |
| P | GLY8 |
| P | PHE9 |
| P | GLY10 |
| P | ARG11 |
| P | ILE12 |
| P | ASP34 |
| P | LEU35 |
| P | LYS78 |
| P | CYS96 |
| P | THR97 |
| P | GLY98 |
| P | SER120 |
| P | ALA121 |
| P | THR180 |
| P | ASN315 |
| P | PHE319 |
| P | G3H402 |
| P | HOH501 |
| P | HOH502 |
| P | HOH513 |
| P | HOH520 |
| P | HOH531 |
| P | HOH534 |
| P | HOH542 |
| P | HOH546 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue G3H P 402 |
| Chain | Residue |
| P | SER149 |
| P | SER150 |
| P | THR151 |
| P | HIS177 |
| P | THR180 |
| P | THR182 |
| P | ARG232 |
| P | NAD401 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 P 403 |
| Chain | Residue |
| P | HIS163 |
| P | GLY167 |
| P | ILE168 |
| P | LEU222 |
| P | LYS225 |
| site_id | AC8 |
| Number of Residues | 30 |
| Details | binding site for residue NAD Q 401 |
| Chain | Residue |
| Q | LYS78 |
| Q | CYS96 |
| Q | THR97 |
| Q | GLY98 |
| Q | PHE99 |
| Q | SER120 |
| Q | ALA121 |
| Q | SER150 |
| Q | THR180 |
| Q | ASN315 |
| Q | PHE319 |
| Q | 3PG402 |
| Q | HOH502 |
| Q | HOH512 |
| Q | HOH522 |
| Q | HOH526 |
| Q | HOH531 |
| Q | HOH552 |
| Q | HOH555 |
| Q | HOH562 |
| Q | HOH577 |
| Q | HOH581 |
| Q | ASN7 |
| Q | GLY8 |
| Q | PHE9 |
| Q | GLY10 |
| Q | ARG11 |
| Q | ILE12 |
| Q | ASP34 |
| Q | LEU35 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue 3PG Q 402 |
| Chain | Residue |
| Q | SER149 |
| Q | SER150 |
| Q | THR151 |
| Q | HIS177 |
| Q | THR180 |
| Q | THR182 |
| Q | THR209 |
| Q | ARG232 |
| Q | NAD401 |
| Q | HOH512 |
| Q | HOH553 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 Q 403 |
| Chain | Residue |
| Q | HIS163 |
| Q | GLY167 |
| Q | ILE168 |
| Q | GLU221 |
| Q | LEU222 |
| Q | LYS225 |
| site_id | AD2 |
| Number of Residues | 26 |
| Details | binding site for residue NAD R 401 |
| Chain | Residue |
| R | ASN7 |
| R | GLY8 |
| R | PHE9 |
| R | GLY10 |
| R | ARG11 |
| R | ILE12 |
| R | ASN33 |
| R | ASP34 |
| R | LYS78 |
| R | CYS96 |
| R | THR97 |
| R | GLY98 |
| R | PHE99 |
| R | SER120 |
| R | ALA121 |
| R | THR180 |
| R | ASN315 |
| R | PHE319 |
| R | 3PG402 |
| R | HOH501 |
| R | HOH503 |
| R | HOH513 |
| R | HOH525 |
| R | HOH529 |
| R | HOH553 |
| R | HOH558 |
| site_id | AD3 |
| Number of Residues | 11 |
| Details | binding site for residue 3PG R 402 |
| Chain | Residue |
| R | SER149 |
| R | SER150 |
| R | THR151 |
| R | HIS177 |
| R | THR180 |
| R | THR182 |
| R | THR209 |
| R | ARG232 |
| R | NAD401 |
| R | HOH525 |
| R | HOH545 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 R 403 |
| Chain | Residue |
| R | HIS163 |
| R | GLY167 |
| R | ILE168 |
| R | LYS225 |
Functional Information from PROSITE/UniProt
| site_id | PS00430 |
| Number of Residues | 89 |
| Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. hhhhhhssglvprgshmasmskvgingfgrigrlvlrrllevksnidvvaindltspkilayllkhdsnygpfpwsvdfte..................................DSLIVDGK |
| Chain | Residue | Details |
| O | HIS-18-LYS70 |






