7C5N
Crystal Structure of C150A+H177A mutant of Glyceraldehyde-3-phosphate-dehydrogenase1 from Escherichia coli at 2.0 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 | 35 |
| 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 | ALA150 |
| O | ASN315 |
| O | PHE319 |
| O | GLY8 |
| O | CL405 |
| O | HOH507 |
| O | HOH513 |
| O | HOH564 |
| O | HOH576 |
| O | HOH581 |
| O | HOH587 |
| O | HOH601 |
| O | HOH607 |
| O | HOH609 |
| O | PHE9 |
| O | HOH612 |
| O | HOH644 |
| O | HOH661 |
| O | HOH668 |
| O | HOH669 |
| O | HOH673 |
| O | GLY10 |
| O | ARG11 |
| O | ILE12 |
| O | ASN33 |
| O | ASP34 |
| O | LEU35 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 O 402 |
| Chain | Residue |
| O | ALA201 |
| O | HOH616 |
| O | HOH636 |
| P | ALA201 |
| P | HOH645 |
| Q | ALA201 |
| R | ALA201 |
| R | HOH603 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CL O 403 |
| Chain | Residue |
| O | LYS227 |
| O | GLY228 |
| O | HOH733 |
| O | HOH797 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CL O 404 |
| Chain | Residue |
| O | ALA80 |
| O | LYS81 |
| O | ALA108 |
| O | HOH771 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL O 405 |
| Chain | Residue |
| O | THR180 |
| O | NAD401 |
| O | HOH646 |
| site_id | AC6 |
| Number of Residues | 30 |
| 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 | SER120 |
| P | ALA121 |
| P | ALA150 |
| P | THR180 |
| P | ASN315 |
| P | PHE319 |
| P | CL404 |
| P | HOH502 |
| P | HOH523 |
| P | HOH543 |
| P | HOH597 |
| P | HOH602 |
| P | HOH610 |
| P | HOH622 |
| P | HOH629 |
| P | HOH640 |
| P | HOH655 |
| P | HOH684 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue EDO P 402 |
| Chain | Residue |
| P | GLU62 |
| P | HOH522 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue CL P 403 |
| Chain | Residue |
| P | LYS227 |
| P | GLY228 |
| P | HOH775 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue CL P 404 |
| Chain | Residue |
| P | THR180 |
| P | NAD401 |
| P | HOH603 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue CL P 405 |
| Chain | Residue |
| P | ALA80 |
| P | LYS81 |
| P | ALA108 |
| P | HOH714 |
| site_id | AD2 |
| Number of Residues | 33 |
| Details | binding site for residue NAD Q 401 |
| Chain | Residue |
| Q | ARG11 |
| Q | ILE12 |
| Q | ASN33 |
| Q | ASP34 |
| Q | LYS78 |
| Q | CYS96 |
| Q | THR97 |
| Q | GLY98 |
| Q | PHE99 |
| Q | SER120 |
| Q | ALA121 |
| Q | ALA150 |
| Q | THR180 |
| Q | ASN315 |
| Q | PHE319 |
| Q | CL404 |
| Q | HOH519 |
| Q | HOH524 |
| Q | HOH552 |
| Q | HOH581 |
| Q | HOH584 |
| Q | HOH591 |
| Q | HOH596 |
| Q | HOH604 |
| Q | HOH615 |
| Q | HOH618 |
| Q | HOH621 |
| Q | HOH622 |
| Q | HOH641 |
| Q | HOH643 |
| Q | ASN7 |
| Q | GLY8 |
| Q | GLY10 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue CL Q 402 |
| Chain | Residue |
| Q | LYS227 |
| Q | GLY228 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue CL Q 403 |
| Chain | Residue |
| Q | ALA80 |
| Q | LYS81 |
| Q | HOH716 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue CL Q 404 |
| Chain | Residue |
| Q | THR180 |
| Q | NAD401 |
| Q | HOH535 |
| site_id | AD6 |
| Number of Residues | 33 |
| 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 | LEU35 |
| R | LYS78 |
| R | CYS96 |
| R | THR97 |
| R | GLY98 |
| R | PHE99 |
| R | SER120 |
| R | ALA121 |
| R | ALA150 |
| R | THR180 |
| R | ASN315 |
| R | PHE319 |
| R | HOH513 |
| R | HOH521 |
| R | HOH530 |
| R | HOH550 |
| R | HOH567 |
| R | HOH586 |
| R | HOH587 |
| R | HOH600 |
| R | HOH604 |
| R | HOH609 |
| R | HOH625 |
| R | HOH662 |
| R | HOH666 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue CL R 402 |
| Chain | Residue |
| Q | HOH571 |
| R | LYS227 |
| R | GLY228 |
| R | HOH675 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue CL R 403 |
| Chain | Residue |
| R | THR180 |
| R | THR182 |
| R | HOH550 |
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 |






