7C7K
Crystal Structure of Thioacyl-Glyceraldehyde-3-phosphate dehydrogenase 1(GAPDH 1) from Escherichia coli at 1.77 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 | 11 |
| Details | binding site for residue G3H O 401 |
| Chain | Residue |
| O | SER149 |
| O | HOH599 |
| O | HOH704 |
| O | CYS150 |
| O | THR151 |
| O | HIS177 |
| O | THR180 |
| O | THR209 |
| O | PEG407 |
| O | HOH524 |
| O | HOH531 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 O 402 |
| Chain | Residue |
| O | HIS163 |
| O | GLY167 |
| O | ILE168 |
| O | GLU169 |
| O | LYS225 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO O 403 |
| Chain | Residue |
| O | ASP274 |
| O | GLU275 |
| O | HOH723 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO O 404 |
| Chain | Residue |
| O | ARG19 |
| O | HIS286 |
| O | ARG325 |
| O | HOH652 |
| O | HOH737 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO O 405 |
| Chain | Residue |
| O | GLU77 |
| O | LYS78 |
| O | GLU79 |
| O | ASN82 |
| O | HOH566 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 O 406 |
| Chain | Residue |
| O | ALA201 |
| O | HOH534 |
| O | HOH598 |
| P | ALA201 |
| Q | ALA201 |
| R | ALA201 |
| R | HOH591 |
| R | HOH653 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue PEG O 407 |
| Chain | Residue |
| O | PRO122 |
| O | SER149 |
| O | THR152 |
| O | THR209 |
| O | GLY210 |
| O | ALA211 |
| O | G3H401 |
| O | HOH508 |
| O | HOH512 |
| O | HOH736 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO P 402 |
| Chain | Residue |
| P | SER165 |
| P | PHE166 |
| P | LYS249 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO P 403 |
| Chain | Residue |
| P | ASN315 |
| P | GLU316 |
| P | G3H401 |
| P | HOH505 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue ACN P 404 |
| Chain | Residue |
| P | THR180 |
| P | THR182 |
| P | ARG232 |
| P | G3H401 |
| P | HOH765 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO P 405 |
| Chain | Residue |
| P | ARG19 |
| P | HIS286 |
| P | ARG325 |
| P | HOH513 |
| P | HOH623 |
| P | HOH702 |
| site_id | AD3 |
| Number of Residues | 33 |
| Details | binding site for residue NAD Q 401 |
| Chain | Residue |
| Q | ASN7 |
| Q | GLY8 |
| Q | PHE9 |
| Q | GLY10 |
| Q | ARG11 |
| Q | ILE12 |
| Q | ASN33 |
| Q | ASP34 |
| Q | LEU35 |
| Q | LYS78 |
| Q | CYS96 |
| Q | THR97 |
| Q | GLY98 |
| Q | PHE99 |
| Q | SER120 |
| Q | ALA121 |
| Q | CYS150 |
| Q | THR180 |
| Q | ASN315 |
| Q | PHE319 |
| Q | G3H402 |
| Q | ACN406 |
| Q | HOH502 |
| Q | HOH503 |
| Q | HOH528 |
| Q | HOH550 |
| Q | HOH552 |
| Q | HOH566 |
| Q | HOH610 |
| Q | HOH644 |
| Q | HOH648 |
| Q | HOH672 |
| Q | HOH683 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO Q 403 |
| Chain | Residue |
| Q | GLU268 |
| Q | HIS286 |
| Q | ARG325 |
| Q | HOH567 |
| Q | HOH690 |
| Q | HOH702 |
| Q | ARG19 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO Q 404 |
| Chain | Residue |
| Q | ILE246 |
| Q | LEU247 |
| Q | ASP303 |
| Q | LEU304 |
| Q | GLN305 |
| Q | HOH591 |
| Q | HOH682 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO Q 405 |
| Chain | Residue |
| Q | ASP274 |
| Q | GLU275 |
| Q | HOH592 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue ACN Q 406 |
| Chain | Residue |
| Q | THR180 |
| Q | THR182 |
| Q | ARG232 |
| Q | NAD401 |
| Q | G3H402 |
| Q | HOH566 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO Q 407 |
| Chain | Residue |
| Q | THR264 |
| Q | ASN267 |
| Q | PHE270 |
| Q | GLY271 |
| Q | TYR272 |
| Q | PHE287 |
| Q | HOH620 |
| site_id | AD9 |
| Number of Residues | 8 |
| Details | binding site for residue NAD R 402 |
| Chain | Residue |
| R | GLY10 |
| R | ARG11 |
| R | ILE12 |
| R | CYS96 |
| R | HOH626 |
| R | HOH629 |
| R | HOH654 |
| R | HOH656 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO R 403 |
| Chain | Residue |
| R | ARG19 |
| R | GLU268 |
| R | HIS286 |
| R | ARG325 |
| R | HOH548 |
| R | HOH612 |
| R | HOH664 |
| site_id | AE2 |
| Number of Residues | 2 |
| Details | binding site for residue PEG R 404 |
| Chain | Residue |
| R | GLN107 |
| R | ILE144 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO R 405 |
| Chain | Residue |
| R | ASP274 |
| R | GLU275 |
| R | HOH583 |
| R | HOH604 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue ACN R 406 |
| Chain | Residue |
| R | THR180 |
| R | THR182 |
| R | ARG232 |
| R | G3H401 |
| R | HOH741 |
| site_id | AE5 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide G3H P 401 and CYS P 150 |
| Chain | Residue |
| P | SER149 |
| P | THR151 |
| P | THR152 |
| P | ASN153 |
| P | CYS154 |
| P | HIS177 |
| P | THR180 |
| P | THR209 |
| P | GLY210 |
| P | TYR313 |
| P | ASN315 |
| P | PHE319 |
| P | EDO403 |
| P | ACN404 |
| P | HOH519 |
| P | HOH600 |
| P | HOH611 |
| P | HOH639 |
| P | HOH649 |
| site_id | AE6 |
| Number of Residues | 18 |
| Details | binding site for Di-peptide G3H Q 402 and CYS Q 150 |
| Chain | Residue |
| Q | SER149 |
| Q | THR151 |
| Q | THR152 |
| Q | ASN153 |
| Q | CYS154 |
| Q | HIS177 |
| Q | THR180 |
| Q | THR209 |
| Q | GLY210 |
| Q | TYR313 |
| Q | ASN315 |
| Q | PHE319 |
| Q | NAD401 |
| Q | ACN406 |
| Q | HOH505 |
| Q | HOH534 |
| Q | HOH541 |
| Q | HOH663 |
| site_id | AE7 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide G3H R 401 and CYS R 150 |
| Chain | Residue |
| R | SER149 |
| R | THR151 |
| R | THR152 |
| R | ASN153 |
| R | CYS154 |
| R | HIS177 |
| R | THR180 |
| R | THR209 |
| R | GLY210 |
| R | TYR313 |
| R | ASN315 |
| R | PHE319 |
| R | ACN406 |
| R | HOH515 |
| R | HOH544 |
| R | HOH562 |
| R | HOH566 |
| R | HOH570 |
| R | HOH643 |
Functional Information from PROSITE/UniProt
| site_id | PS00071 |
| Number of Residues | 8 |
| Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
| Chain | Residue | Details |
| O | ALA148-LEU155 |
| 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 |






