6IQM
Crystal Structure of Cell Surface Glyceraldehyde-3-Phosphate Dehydrogenase Complexed with NAD+ from Lactobacillus plantarum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006006 | biological_process | glucose metabolic process |
| 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 | 0006006 | biological_process | glucose metabolic process |
| 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 | 0006006 | biological_process | glucose metabolic process |
| 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 | 0006006 | biological_process | glucose metabolic process |
| 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 | 33 |
| Details | binding site for residue NAD A 401 |
| Chain | Residue |
| A | ASN8 |
| A | GLU81 |
| A | PRO82 |
| A | CYS101 |
| A | THR102 |
| A | GLY103 |
| A | PHE104 |
| A | SER125 |
| A | ALA126 |
| A | GLU323 |
| A | PHE326 |
| A | GLY9 |
| A | HOH505 |
| A | HOH509 |
| A | HOH513 |
| A | HOH522 |
| A | HOH533 |
| A | HOH541 |
| A | HOH555 |
| A | HOH581 |
| A | HOH680 |
| A | HOH691 |
| A | PHE10 |
| A | HOH700 |
| A | HOH718 |
| A | HOH745 |
| A | HOH751 |
| A | GLY11 |
| A | ARG12 |
| A | ILE13 |
| A | ASN37 |
| A | ASP38 |
| A | LEU39 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | HIS47 |
| A | VAL62 |
| A | HOH558 |
| A | HOH577 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | ARG12 |
| A | ARG15 |
| A | ARG19 |
| A | LEU48 |
| A | LEU49 |
| A | ASP52 |
| A | HOH607 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue TRS B 401 |
| Chain | Residue |
| A | GLY208 |
| A | GLY241 |
| A | HOH545 |
| A | HOH593 |
| B | GLY208 |
| B | GLY241 |
| B | HOH518 |
| B | HOH744 |
| C | HOH540 |
| C | HOH583 |
| D | GLY208 |
| D | GLY241 |
| D | HOH530 |
| D | HOH570 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | binding site for residue NAD B 402 |
| Chain | Residue |
| B | ASN8 |
| B | GLY9 |
| B | GLY11 |
| B | ARG12 |
| B | ILE13 |
| B | ASN37 |
| B | ASP38 |
| B | PRO82 |
| B | CYS101 |
| B | THR102 |
| B | GLY103 |
| B | SER125 |
| B | ALA126 |
| B | CYS156 |
| B | SER187 |
| B | ASN322 |
| B | PHE326 |
| B | HOH510 |
| B | HOH514 |
| B | HOH522 |
| B | HOH530 |
| B | HOH537 |
| B | HOH569 |
| B | HOH605 |
| B | HOH639 |
| B | HOH670 |
| B | HOH675 |
| B | HOH679 |
| B | HOH718 |
| D | PRO195 |
| D | HOH631 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | HIS47 |
| B | VAL62 |
| B | HOH534 |
| B | HOH600 |
| B | HOH602 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | binding site for residue NAD C 401 |
| Chain | Residue |
| C | ARG12 |
| C | ILE13 |
| C | ASN37 |
| C | ASP38 |
| C | PRO82 |
| C | CYS101 |
| C | THR102 |
| C | GLY103 |
| C | PHE104 |
| C | SER125 |
| C | ALA126 |
| C | CYS156 |
| C | SER187 |
| C | ASN322 |
| C | PHE326 |
| C | HOH531 |
| C | HOH532 |
| C | HOH551 |
| C | HOH584 |
| C | HOH594 |
| C | HOH595 |
| C | HOH614 |
| C | HOH625 |
| C | HOH637 |
| C | HOH661 |
| C | HOH672 |
| C | HOH684 |
| A | PRO195 |
| A | HOH634 |
| C | ASN8 |
| C | GLY9 |
| C | GLY11 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 402 |
| Chain | Residue |
| C | HIS47 |
| C | VAL62 |
| C | HOH582 |
| C | HOH597 |
| C | HOH598 |
| site_id | AC9 |
| Number of Residues | 32 |
| Details | binding site for residue NAD D 401 |
| Chain | Residue |
| B | PRO195 |
| B | HOH624 |
| D | ASN8 |
| D | GLY9 |
| D | PHE10 |
| D | GLY11 |
| D | ARG12 |
| D | ILE13 |
| D | ASN37 |
| D | ASP38 |
| D | PRO82 |
| D | CYS101 |
| D | THR102 |
| D | GLY103 |
| D | PHE104 |
| D | SER125 |
| D | ALA126 |
| D | CYS156 |
| D | ASN322 |
| D | PHE326 |
| D | HOH528 |
| D | HOH549 |
| D | HOH566 |
| D | HOH573 |
| D | HOH600 |
| D | HOH611 |
| D | HOH627 |
| D | HOH635 |
| D | HOH655 |
| D | HOH688 |
| D | HOH700 |
| D | HOH739 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 402 |
| Chain | Residue |
| D | HIS47 |
| D | VAL62 |
| D | HOH551 |
| D | HOH601 |
| D | HOH623 |
