1GAD
COMPARISON OF THE STRUCTURES OF WILD TYPE AND A N313T MUTANT OF ESCHERICHIA COLI GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASES: IMPLICATION FOR NAD BINDING AND COOPERATIVITY
Functional Information from GO Data
Chain | GOid | namespace | contents |
O | 0000166 | molecular_function | nucleotide binding |
O | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
O | 0005515 | molecular_function | protein binding |
O | 0005737 | cellular_component | cytoplasm |
O | 0005829 | cellular_component | cytosol |
O | 0006006 | biological_process | glucose metabolic process |
O | 0006096 | biological_process | glycolytic process |
O | 0016020 | cellular_component | membrane |
O | 0016491 | molecular_function | oxidoreductase activity |
O | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
O | 0042802 | molecular_function | identical protein binding |
O | 0050661 | molecular_function | NADP binding |
O | 0051287 | molecular_function | NAD binding |
P | 0000166 | molecular_function | nucleotide binding |
P | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
P | 0005515 | molecular_function | protein binding |
P | 0005737 | cellular_component | cytoplasm |
P | 0005829 | cellular_component | cytosol |
P | 0006006 | biological_process | glucose metabolic process |
P | 0006096 | biological_process | glycolytic process |
P | 0016020 | cellular_component | membrane |
P | 0016491 | molecular_function | oxidoreductase activity |
P | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
P | 0042802 | molecular_function | identical protein binding |
P | 0050661 | molecular_function | NADP binding |
P | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD O 336 |
Chain | Residue |
O | GLY9 |
O | LEU98 |
O | THR119 |
O | CYS149 |
O | ASN313 |
O | TYR317 |
O | HOH344 |
O | HOH345 |
O | HOH347 |
O | HOH356 |
O | HOH359 |
O | ARG10 |
O | HOH366 |
O | HOH383 |
O | HOH384 |
O | HOH460 |
O | ILE11 |
O | ASN31 |
O | ASP32 |
O | ARG77 |
O | ALA95 |
O | THR96 |
O | GLY97 |
site_id | AC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAD P 336 |
Chain | Residue |
P | GLY7 |
P | GLY9 |
P | ARG10 |
P | ILE11 |
P | ASN31 |
P | ASP32 |
P | ARG77 |
P | ALA95 |
P | THR96 |
P | GLY97 |
P | LEU98 |
P | THR119 |
P | ALA180 |
P | ASN313 |
P | TYR317 |
P | HOH350 |
P | HOH351 |
P | HOH353 |
P | HOH366 |
P | HOH372 |
P | HOH378 |
P | HOH394 |
P | HOH421 |
P | HOH456 |
P | HOH483 |
Functional Information from PROSITE/UniProt
site_id | PS00071 |
Number of Residues | 8 |
Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
Chain | Residue | Details |
O | ALA147-LEU154 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:10978154 |
Chain | Residue | Details |
O | THR150 | |
P | THR150 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984, ECO:0000269|Ref.18 |
Chain | Residue | Details |
O | ILE11 | |
P | ILE11 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984 |
Chain | Residue | Details |
O | LEU33 | |
O | GLU314 | |
P | LEU33 | |
P | GLU314 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219 |
Chain | Residue | Details |
O | ASP78 | |
P | ASP78 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19542219 |
Chain | Residue | Details |
O | GLY120 | |
P | GLY120 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10978154 |
Chain | Residue | Details |
O | CYS149 | |
O | GLY209 | |
P | CYS149 | |
P | GLY209 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00362 |
Chain | Residue | Details |
O | ALA180 | |
P | ALA180 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19542219, ECO:0000269|Ref.18, ECO:0000305|PubMed:10978154 |
Chain | Residue | Details |
O | VAL232 | |
P | VAL232 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | SITE: Activates thiol group during catalysis => ECO:0000269|PubMed:2659073 |
Chain | Residue | Details |
O | ALA177 | |
P | ALA177 |
site_id | SWS_FT_FI10 |
Number of Residues | 16 |
Details | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
O | LYS115 | |
P | ASP123 | |
P | ALA213 | |
P | VAL217 | |
P | LEU225 | |
P | ALA249 | |
P | ALA257 | |
P | ALA261 | |
O | ASP123 | |
O | ALA213 | |
O | VAL217 | |
O | LEU225 | |
O | ALA249 | |
O | ALA257 | |
O | ALA261 | |
P | LYS115 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
O | GLY131 | |
O | ASP192 | |
P | GLY131 | |
P | ASP192 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
O | TYR137 | |
P | TYR137 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
O | CYS149 | |
O | HIS176 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
P | CYS149 | |
P | HIS176 |