2VYV
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 |
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 |
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 |
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 | 7 |
Details | BINDING SITE FOR RESIDUE 1GP D1334 |
Chain | Residue |
D | CSD149 |
D | HIS176 |
D | THR179 |
D | THR181 |
D | ARG231 |
D | NAD1340 |
D | HOH2210 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT A1330 |
Chain | Residue |
A | LYS215 |
A | HOH2208 |
A | MET127 |
A | ASN133 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT C1330 |
Chain | Residue |
C | PRO126 |
C | MET127 |
C | HOH2183 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT D1335 |
Chain | Residue |
D | MET126 |
D | HOH2211 |
D | HOH2212 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT B1330 |
Chain | Residue |
B | PRO126 |
B | MET127 |
B | LYS215 |
B | HOH2197 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT D1336 |
Chain | Residue |
C | GLU285 |
C | HOH2148 |
D | ARG51 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT B1331 |
Chain | Residue |
A | ARG51 |
B | ASN283 |
B | GLU285 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FMT D1337 |
Chain | Residue |
D | PRO120 |
D | SER148 |
D | THR151 |
D | GLY209 |
D | ALA210 |
D | ALA213 |
D | HOH2213 |
D | HOH2214 |
D | HOH2215 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT D1338 |
Chain | Residue |
D | GLY130 |
D | GLU133 |
D | PRO266 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A1331 |
Chain | Residue |
A | ARG51 |
B | THR273 |
B | GLU285 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT B1332 |
Chain | Residue |
B | THR273 |
B | GLU274 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A1332 |
Chain | Residue |
A | GLY131 |
A | ALA132 |
A | PHE134 |
A | HOH2209 |
A | HOH2210 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT B1333 |
Chain | Residue |
B | GLY131 |
B | PHE134 |
B | ASP135 |
B | HOH2069 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT D1339 |
Chain | Residue |
D | ARG17 |
D | HOH2216 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT C1331 |
Chain | Residue |
C | GLY131 |
C | ALA132 |
C | ASN133 |
C | PHE134 |
site_id | BC7 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD A1333 |
Chain | Residue |
A | GLY7 |
A | PHE8 |
A | GLY9 |
A | ARG10 |
A | ILE11 |
A | ASN31 |
A | ASP32 |
A | ARG76 |
A | ALA94 |
A | THR95 |
A | GLY96 |
A | LEU97 |
A | THR118 |
A | CSD148 |
A | ALA179 |
A | ASN312 |
A | HOH2097 |
A | HOH2211 |
A | HOH2213 |
A | HOH2214 |
A | HOH2216 |
A | HOH2217 |
A | HOH2218 |
A | HOH2219 |
site_id | BC8 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAD B1334 |
Chain | Residue |
B | GLU313 |
B | TYR316 |
B | HOH2049 |
B | HOH2187 |
B | HOH2198 |
B | HOH2200 |
B | HOH2202 |
B | HOH2203 |
B | HOH2204 |
B | HOH2205 |
B | HOH2206 |
B | HOH2207 |
C | PRO187 |
B | ASN6 |
B | GLY9 |
B | ARG10 |
B | ILE11 |
B | ASN31 |
B | ASP32 |
B | LEU33 |
B | ARG76 |
B | ALA94 |
B | THR95 |
B | GLY96 |
B | LEU97 |
B | THR118 |
B | CSD148 |
B | ALA179 |
B | ASN312 |
site_id | BC9 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD C1332 |
Chain | Residue |
C | GLY7 |
C | PHE8 |
C | GLY9 |
C | ARG10 |
C | ILE11 |
C | ASN31 |
C | ASP32 |
C | ARG76 |
C | ALA94 |
C | THR95 |
C | GLY96 |
C | LEU97 |
C | THR118 |
C | CSD148 |
C | ALA179 |
C | ASN312 |
C | TYR316 |
C | HOH2003 |
C | HOH2050 |
C | HOH2057 |
C | HOH2075 |
C | HOH2087 |
C | HOH2185 |
C | HOH2186 |
C | HOH2187 |
C | HOH2188 |
C | HOH2189 |
C | HOH2190 |
site_id | CC1 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAD D1340 |
Chain | Residue |
A | HOH2117 |
D | ASN6 |
D | GLY7 |
D | PHE8 |
D | GLY9 |
D | ARG10 |
D | ILE11 |
D | ASN30 |
D | ASP31 |
D | PRO32 |
D | PHE33 |
D | LYS76 |
D | ALA94 |
D | THR95 |
D | GLY96 |
D | TYR98 |
D | THR118 |
D | ALA119 |
D | CSD149 |
D | ALA180 |
D | ASN313 |
D | TYR317 |
D | 1GP1334 |
D | HOH2063 |
D | HOH2115 |
D | HOH2210 |
D | HOH2217 |
D | HOH2218 |
D | HOH2219 |
D | HOH2220 |
D | HOH2221 |
D | HOH2222 |
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 |