3B1J
Crystal structure of Glyceraldehyde-3-Phosphate Dehydrogenase complexed with CP12 in the presence of copper from Synechococcus elongatus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
A | 0005829 | cellular_component | cytosol |
A | 0006006 | biological_process | glucose metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
A | 0046872 | molecular_function | metal ion binding |
A | 0048046 | cellular_component | apoplast |
A | 0050661 | molecular_function | NADP binding |
A | 0051287 | molecular_function | NAD binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
B | 0005829 | cellular_component | cytosol |
B | 0006006 | biological_process | glucose metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
B | 0046872 | molecular_function | metal ion binding |
B | 0048046 | cellular_component | apoplast |
B | 0050661 | molecular_function | NADP binding |
B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAD A 340 |
Chain | Residue |
A | GLY9 |
A | SER98 |
A | THR99 |
A | GLY100 |
A | THR122 |
A | ALA123 |
A | CYS155 |
A | LEU186 |
A | ASN318 |
A | TYR322 |
A | HOH343 |
A | PHE10 |
A | HOH345 |
A | HOH353 |
A | HOH358 |
A | HOH365 |
A | HOH372 |
A | HOH389 |
A | HOH412 |
A | HOH421 |
C | TYR73 |
C | HOH108 |
A | GLY11 |
A | ARG12 |
A | ILE13 |
A | ASN35 |
A | ASN36 |
A | THR37 |
A | ARG80 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CU A 341 |
Chain | Residue |
A | CYS155 |
A | THR156 |
C | ASP75 |
site_id | AC3 |
Number of Residues | 29 |
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 | ARG80 |
B | SER98 |
B | THR99 |
B | GLY100 |
B | THR122 |
B | ALA123 |
B | CYS155 |
B | LEU186 |
B | ASN318 |
B | TYR322 |
B | HOH343 |
B | HOH354 |
B | HOH358 |
B | HOH402 |
B | HOH403 |
B | HOH409 |
B | HOH410 |
B | HOH437 |
D | ASP66 |
D | TYR73 |
D | ASP74 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU B 341 |
Chain | Residue |
B | CYS155 |
B | THR156 |
B | HIS182 |
D | ASP75 |
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 |