7C5O
Crystal Structure of H177A mutant of Glyceraldehyde-3-phosphate-dehydrogenase1 from Escherichia coli complexed with NAD at 1.98 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 | 31 |
| 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 | CYS150 |
| O | ASN315 |
| O | PHE319 |
| O | GLY8 |
| O | HOH511 |
| O | HOH514 |
| O | HOH524 |
| O | HOH594 |
| O | HOH633 |
| O | HOH653 |
| O | HOH656 |
| O | HOH667 |
| O | HOH677 |
| O | HOH690 |
| O | PHE9 |
| O | HOH694 |
| O | HOH708 |
| O | GLY10 |
| O | ARG11 |
| O | ILE12 |
| O | ASN33 |
| O | ASP34 |
| O | LEU35 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 O 402 |
| Chain | Residue |
| O | ALA201 |
| O | HOH574 |
| P | ALA201 |
| Q | ALA201 |
| R | ALA201 |
| R | HOH610 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL O 403 |
| Chain | Residue |
| O | LYS213 |
| O | LYS227 |
| O | GLY228 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CL O 404 |
| Chain | Residue |
| O | ALA80 |
| O | LYS81 |
| O | ALA108 |
| O | HOH582 |
| O | HOH768 |
| O | HOH820 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | binding site for residue NAD P 401 |
| Chain | Residue |
| P | ASN7 |
| P | GLY8 |
| P | PHE9 |
| P | GLY10 |
| P | ARG11 |
| P | ILE12 |
| P | ASN33 |
| P | ASP34 |
| P | LYS78 |
| P | CYS96 |
| P | THR97 |
| P | GLY98 |
| P | PHE99 |
| P | SER120 |
| P | ALA121 |
| P | CYS150 |
| P | ASN315 |
| P | PHE319 |
| P | HOH502 |
| P | HOH508 |
| P | HOH512 |
| P | HOH591 |
| P | HOH602 |
| P | HOH616 |
| P | HOH620 |
| P | HOH628 |
| P | HOH631 |
| P | HOH634 |
| P | HOH653 |
| P | HOH695 |
| Q | HOH562 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL P 402 |
| Chain | Residue |
| P | LYS213 |
| P | LYS227 |
| P | GLY228 |
| P | HOH775 |
| site_id | AC7 |
| Number of Residues | 31 |
| Details | binding site for residue NAD Q 401 |
| Chain | Residue |
| Q | HOH537 |
| Q | HOH548 |
| Q | HOH567 |
| Q | HOH574 |
| Q | HOH585 |
| Q | HOH607 |
| Q | HOH618 |
| Q | HOH620 |
| Q | HOH633 |
| Q | HOH648 |
| Q | HOH674 |
| Q | HOH678 |
| Q | HOH679 |
| Q | ASN7 |
| Q | GLY8 |
| 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 | ASN315 |
| Q | PHE319 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue CL Q 402 |
| Chain | Residue |
| Q | LYS227 |
| Q | GLY228 |
| Q | HOH774 |
| site_id | AC9 |
| Number of Residues | 27 |
| Details | binding site for residue NAD R 401 |
| Chain | Residue |
| R | GLY8 |
| R | GLY10 |
| R | ARG11 |
| R | ILE12 |
| R | ASP34 |
| R | LEU35 |
| R | LYS78 |
| R | CYS96 |
| R | THR97 |
| R | GLY98 |
| R | PHE99 |
| R | SER120 |
| R | ALA121 |
| R | CYS150 |
| R | ASN315 |
| R | PHE319 |
| R | HOH512 |
| R | HOH520 |
| R | HOH537 |
| R | HOH539 |
| R | HOH544 |
| R | HOH570 |
| R | HOH573 |
| R | HOH584 |
| R | HOH605 |
| R | HOH607 |
| R | HOH632 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue CL R 402 |
| Chain | Residue |
| R | LYS227 |
| R | GLY228 |
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 |






