2YYY
Crystal structure of Glyceraldehyde-3-phosphate dehydrogenase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006096 | biological_process | glycolytic 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 | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity |
A | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
A | 0050661 | molecular_function | NADP binding |
A | 0051287 | molecular_function | NAD binding |
B | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006096 | biological_process | glycolytic 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 | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity |
B | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
B | 0050661 | molecular_function | NADP binding |
B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAP B 1001 |
Chain | Residue |
B | ASN8 |
B | ALA54 |
B | GLY88 |
B | ALA89 |
B | PRO90 |
B | ILE93 |
B | ASN97 |
B | GLN112 |
B | GLY114 |
B | CYS144 |
B | ARG172 |
B | GLY9 |
B | ASP175 |
B | GLN307 |
B | HOH1004 |
B | HOH1005 |
B | HOH1062 |
B | HOH1075 |
B | HOH1119 |
B | HOH1127 |
B | HOH1142 |
B | TYR10 |
B | GLY11 |
B | SER12 |
B | ILE13 |
B | LYS34 |
B | THR35 |
B | LYS36 |
site_id | AC2 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAP A 2001 |
Chain | Residue |
A | ASN8 |
A | GLY9 |
A | TYR10 |
A | GLY11 |
A | SER12 |
A | ILE13 |
A | LYS34 |
A | THR35 |
A | LYS36 |
A | ALA54 |
A | GLY88 |
A | ALA89 |
A | PRO90 |
A | ILE93 |
A | ASN97 |
A | GLN112 |
A | GLY114 |
A | CYS144 |
A | ARG172 |
A | ASP175 |
A | GLN307 |
A | HOH2025 |
A | HOH2038 |
A | HOH2045 |
A | HOH2099 |
A | HOH2100 |
A | HOH2105 |
A | HOH2112 |
Functional Information from PROSITE/UniProt
site_id | PS00071 |
Number of Residues | 8 |
Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. VSCNTTgL |
Chain | Residue | Details |
A | VAL142-LEU149 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
A | CYS144 | |
B | CYS144 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | SER12 | |
B | ARG172 | |
B | HIS198 | |
B | GLN307 | |
A | GLY114 | |
A | SER143 | |
A | ARG172 | |
A | HIS198 | |
A | GLN307 | |
B | SER12 | |
B | GLY114 | |
B | SER143 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
A | HIS226 | |
A | CYS144 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
B | HIS226 | |
B | CYS144 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
A | CYS144 | |
A | ARG171 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
B | CYS144 | |
B | ARG171 |