3B1K
Crystal structure of Glyceraldehyde-3-Phosphate Dehydrogenase complexed with CP12 in the absence of copper from Synechococcus elongatus
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 | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity |
| 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 | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| G | 0006006 | biological_process | glucose metabolic process |
| G | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| G | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity |
| G | 0050661 | molecular_function | NADP binding |
| G | 0051287 | molecular_function | NAD binding |
| H | 0006006 | biological_process | glucose metabolic process |
| H | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| H | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity |
| H | 0050661 | molecular_function | NADP binding |
| H | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD A 340 |
| Chain | Residue |
| A | GLY11 |
| A | GLY100 |
| A | VAL101 |
| A | PHE102 |
| A | THR122 |
| A | ALA123 |
| A | CYS155 |
| A | LEU186 |
| A | ASN318 |
| A | GLU319 |
| C | TYR73 |
| A | ARG12 |
| H | SER194 |
| J | GLU69 |
| A | ILE13 |
| A | ASN35 |
| A | ASN36 |
| A | THR37 |
| A | ARG80 |
| A | SER98 |
| A | THR99 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD B 340 |
| Chain | Residue |
| B | GLY9 |
| B | PHE10 |
| B | GLY11 |
| B | ARG12 |
| B | ILE13 |
| B | ASN35 |
| B | ASN36 |
| B | THR37 |
| B | ASP79 |
| B | ARG80 |
| B | SER98 |
| B | THR99 |
| B | GLY100 |
| B | THR122 |
| B | CYS155 |
| B | LEU186 |
| B | ASN318 |
| D | ASP66 |
| D | TYR73 |
| D | ASP75 |
| I | GLU69 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD G 340 |
| Chain | Residue |
| B | SER194 |
| G | ASN8 |
| G | GLY9 |
| G | PHE10 |
| G | GLY11 |
| G | ARG12 |
| G | ILE13 |
| G | ASN35 |
| G | ASN36 |
| G | THR37 |
| G | ASP79 |
| G | SER98 |
| G | THR99 |
| G | GLY100 |
| G | PHE102 |
| G | THR122 |
| G | ALA123 |
| G | CYS155 |
| G | LEU186 |
| G | ASN318 |
| G | GLU319 |
| I | TYR73 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAD H 340 |
| Chain | Residue |
| H | GLY9 |
| H | GLY11 |
| H | ARG12 |
| H | ILE13 |
| H | ASN35 |
| H | ASN36 |
| H | THR37 |
| H | ARG80 |
| H | SER98 |
| H | THR99 |
| H | GLY100 |
| H | THR122 |
| H | ALA123 |
| H | CYS155 |
| H | LEU186 |
| H | ASN318 |
| H | GLU319 |
| H | TYR322 |
| J | TYR73 |
Functional Information from PROSITE/UniProt
| site_id | PS00071 |
| Number of Residues | 8 |
| Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
| Chain | Residue | Details |
| A | ALA153-LEU160 |
