5ZA0
A cryo-protectant induces the conformational change of glyceraldehyde-3-phosphate dehydrogenase
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 |
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 | ALA148-LEU155 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:10978154 |
| Chain | Residue | Details |
| A | CYS150 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984, ECO:0000269|Ref.18 |
| Chain | Residue | Details |
| A | ARG12 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984 |
| Chain | Residue | Details |
| A | ASP34 | |
| A | ASN314 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219 |
| Chain | Residue | Details |
| A | ARG78 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19542219 |
| Chain | Residue | Details |
| A | THR120 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10978154 |
| Chain | Residue | Details |
| A | SER149 | |
| A | THR209 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00362 |
| Chain | Residue | Details |
| A | THR180 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19542219, ECO:0000269|Ref.18, ECO:0000305|PubMed:10978154 |
| Chain | Residue | Details |
| A | ARG232 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | SITE: Activates thiol group during catalysis => ECO:0000269|PubMed:2659073 |
| Chain | Residue | Details |
| A | HIS177 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122 |
| Chain | Residue | Details |
| A | LYS115 | |
| A | LYS124 | |
| A | LYS213 | |
| A | LYS217 | |
| A | LYS225 | |
| A | LYS249 | |
| A | LYS257 | |
| A | LYS261 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 |
| Chain | Residue | Details |
| A | LYS132 | |
| A | LYS192 | |
| A | LYS331 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS138 |
