2VYN
Structure of E.Coli GAPDH Rat Sperm GAPDH heterotetramer
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 | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016020 | cellular_component | membrane |
| 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 | 0042802 | molecular_function | identical protein binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| A | 0072524 | biological_process | pyridine-containing compound metabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016020 | cellular_component | membrane |
| 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 | 0042802 | molecular_function | identical protein binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| B | 0072524 | biological_process | pyridine-containing compound metabolic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006006 | biological_process | glucose metabolic process |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
| C | 0072524 | biological_process | pyridine-containing compound metabolic process |
| 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 | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A1332 |
| Chain | Residue |
| A | PRO126 |
| A | MET127 |
| A | ASN133 |
| A | LYS215 |
| A | HOH2205 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT C1332 |
| Chain | Residue |
| C | PRO126 |
| C | MET127 |
| C | LYS215 |
| C | HOH2180 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT D1336 |
| Chain | Residue |
| D | MET126 |
| D | HOH2209 |
| D | HOH2210 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT B1332 |
| Chain | Residue |
| B | PRO126 |
| B | MET127 |
| B | LYS215 |
| B | HOH2201 |
| B | HOH2202 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT D1337 |
| Chain | Residue |
| C | GLU285 |
| D | ARG51 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B1333 |
| Chain | Residue |
| A | ARG51 |
| B | ASP281 |
| B | GLU285 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FMT D1338 |
| Chain | Residue |
| D | PRO120 |
| D | SER148 |
| D | THR151 |
| D | GLY209 |
| D | ALA210 |
| D | ALA213 |
| D | HOH2211 |
| D | HOH2212 |
| D | HOH2214 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT D1339 |
| Chain | Residue |
| D | GLY130 |
| D | GLU133 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT A1333 |
| Chain | Residue |
| A | ARG51 |
| B | THR273 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B1334 |
| Chain | Residue |
| B | THR273 |
| B | GLU274 |
| B | ASP275 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A1334 |
| Chain | Residue |
| A | GLY131 |
| A | ALA132 |
| A | PHE134 |
| A | ASP135 |
| A | HOH2206 |
| A | HOH2207 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT B1335 |
| Chain | Residue |
| B | GLY131 |
| B | ALA132 |
| B | ASN133 |
| B | PHE134 |
| B | ASP135 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT D1340 |
| Chain | Residue |
| D | ARG17 |
| D | GLU21 |
| D | HIS49 |
| D | HOH2215 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT C1333 |
| Chain | Residue |
| C | GLY131 |
| C | ALA132 |
| C | ASN133 |
| C | PHE134 |
| site_id | BC6 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD A1335 |
| Chain | Residue |
| A | ASN6 |
| A | GLY7 |
| A | PHE8 |
| A | GLY9 |
| A | ARG10 |
| A | ILE11 |
| A | ASN31 |
| A | ASP32 |
| A | LEU33 |
| A | GLU75 |
| A | ARG76 |
| A | ALA94 |
| A | THR95 |
| A | GLY96 |
| A | LEU97 |
| A | THR118 |
| A | CSD148 |
| A | ALA179 |
| A | ASN312 |
| A | TYR316 |
| A | HOH2002 |
| A | HOH2066 |
| A | HOH2103 |
| A | HOH2192 |
| A | HOH2208 |
| A | HOH2209 |
| A | HOH2210 |
| A | HOH2211 |
| A | HOH2213 |
| A | HOH2214 |
| A | HOH2215 |
| A | HOH2216 |
| D | PRO188 |
| site_id | BC7 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD B1336 |
| Chain | Residue |
| B | GLU75 |
| B | ARG76 |
| B | ALA94 |
| B | THR95 |
| B | GLY96 |
| B | LEU97 |
| B | THR118 |
| B | CSD148 |
| B | ALA179 |
| B | ASN312 |
| B | TYR316 |
| B | HOH2002 |
| B | HOH2095 |
| B | HOH2186 |
| B | HOH2203 |
| B | HOH2204 |
| B | HOH2206 |
| B | HOH2207 |
| B | HOH2208 |
| B | HOH2209 |
| B | HOH2210 |
| B | HOH2211 |
| C | PRO187 |
| B | ASN6 |
| B | GLY7 |
| B | PHE8 |
| B | GLY9 |
| B | ARG10 |
| B | ILE11 |
| B | ASN31 |
| B | ASP32 |
| B | LEU33 |
| site_id | BC8 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD C1334 |
| Chain | Residue |
| B | PRO187 |
| C | ASN6 |
| C | GLY7 |
| C | PHE8 |
| C | GLY9 |
| C | ARG10 |
| C | ILE11 |
| C | ASN31 |
| C | ASP32 |
| C | LEU33 |
| C | ARG76 |
| C | ALA94 |
| C | THR95 |
| C | GLY96 |
| C | LEU97 |
| C | PHE98 |
| C | THR118 |
| C | CSD148 |
| C | ALA179 |
| C | ASN312 |
| C | TYR316 |
| C | HOH2002 |
| C | HOH2167 |
| C | HOH2177 |
| C | HOH2182 |
| C | HOH2183 |
| C | HOH2184 |
| C | HOH2185 |
| C | HOH2186 |
| C | HOH2187 |
| C | HOH2188 |
| C | HOH2189 |
| site_id | BC9 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD D1341 |
| Chain | Residue |
| D | ASN6 |
| D | GLY7 |
| D | PHE8 |
| D | GLY9 |
| D | ARG10 |
| D | ILE11 |
| D | ASN30 |
| D | ASP31 |
| D | PRO32 |
| D | PHE33 |
| D | CSX75 |
| D | LYS76 |
| D | ALA94 |
| D | THR95 |
| D | GLY96 |
| D | THR118 |
| D | ALA119 |
| D | CSD149 |
| D | ALA180 |
| D | ASN313 |
| D | TYR317 |
| D | HOH2107 |
| D | HOH2199 |
| D | HOH2216 |
| D | HOH2217 |
| D | HOH2218 |
| D | HOH2219 |
| D | HOH2220 |
| D | HOH2221 |
| D | HOH2222 |
| D | HOH2223 |
| D | HOH2224 |
| D | HOH2225 |
| D | HOH2226 |
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 | ALA146-LEU153 | |
| D | ALA147-LEU154 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10009 |
| Chain | Residue | Details |
| D | CSD149 | |
| B | CSD148 | |
| C | CSD148 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| D | ARG10 | |
| D | ASN313 | |
| D | ASP31 | |
| D | LYS76 | |
| D | TYR98 | |
| D | THR118 | |
| D | SER148 | |
| D | THR179 | |
| D | THR208 | |
| D | ARG231 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Activates thiol group during catalysis => ECO:0000250 |
| Chain | Residue | Details |
| D | HIS176 | |
| A | ASN312 | |
| B | ASP32 | |
| B | ASN312 | |
| C | ASP32 | |
| C | ASN312 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| D | SER251 | |
| B | ARG76 | |
| C | ARG76 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19542219 |
| Chain | Residue | Details |
| A | THR118 | |
| B | THR118 | |
| C | THR118 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10978154 |
| Chain | Residue | Details |
| A | SER147 | |
| A | THR207 | |
| B | SER147 | |
| B | THR207 | |
| C | SER147 | |
| C | THR207 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00362 |
| Chain | Residue | Details |
| A | THR178 | |
| B | THR178 | |
| C | THR178 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19542219, ECO:0000269|Ref.18, ECO:0000305|PubMed:10978154 |
| Chain | Residue | Details |
| A | ARG230 | |
| B | ARG230 | |
| C | ARG230 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | SITE: Activates thiol group during catalysis => ECO:0000269|PubMed:2659073 |
| Chain | Residue | Details |
| A | HIS175 | |
| B | HIS175 | |
| C | HIS175 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 24 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122 |
| Chain | Residue | Details |
| A | LYS113 | |
| B | LYS122 | |
| B | LYS211 | |
| B | LYS215 | |
| B | LYS223 | |
| B | LYS247 | |
| B | LYS255 | |
| B | LYS259 | |
| C | LYS113 | |
| C | LYS122 | |
| C | LYS211 | |
| A | LYS122 | |
| C | LYS215 | |
| C | LYS223 | |
| C | LYS247 | |
| C | LYS255 | |
| C | LYS259 | |
| A | LYS211 | |
| A | LYS215 | |
| A | LYS223 | |
| A | LYS247 | |
| A | LYS255 | |
| A | LYS259 | |
| B | LYS113 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 9 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 |
| Chain | Residue | Details |
| A | LYS130 | |
| A | LYS190 | |
| A | LYS329 | |
| B | LYS130 | |
| B | LYS190 | |
| B | LYS329 | |
| C | LYS130 | |
| C | LYS190 | |
| C | LYS329 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS136 | |
| B | LYS136 | |
| C | LYS136 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| D | HIS176 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| A | HIS175 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| B | HIS175 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| C | HIS175 |
