1WPQ
Ternary Complex Of Glycerol 3-phosphate Dehydrogenase 1 with NAD and dihydroxyactone
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006072 | biological_process | glycerol-3-phosphate metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046168 | biological_process | glycerol-3-phosphate catabolic process |
| A | 0047952 | molecular_function | glycerol-3-phosphate dehydrogenase [NAD(P)+] activity |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0141152 | molecular_function | glycerol-3-phosphate dehydrogenase (NAD+) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006072 | biological_process | glycerol-3-phosphate metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046168 | biological_process | glycerol-3-phosphate catabolic process |
| B | 0047952 | molecular_function | glycerol-3-phosphate dehydrogenase [NAD(P)+] activity |
| B | 0051287 | molecular_function | NAD binding |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0141152 | molecular_function | glycerol-3-phosphate dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1001 |
| Chain | Residue |
| A | LYS20 |
| A | GLY66 |
| A | HIS67 |
| A | LYS68 |
| A | HOH3042 |
| A | HOH3047 |
| A | HOH3135 |
| A | HOH3175 |
| A | HOH3245 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1002 |
| Chain | Residue |
| A | HOH3132 |
| A | HOH3195 |
| A | HOH3293 |
| B | LYS20 |
| B | HIS67 |
| B | LYS68 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1003 |
| Chain | Residue |
| A | ARG271 |
| A | LYS272 |
| A | HOH3214 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1004 |
| Chain | Residue |
| A | LYS178 |
| A | GLN182 |
| A | ARG187 |
| A | HOH3102 |
| A | HOH3256 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1005 |
| Chain | Residue |
| B | LYS240 |
| B | VAL247 |
| B | SER248 |
| B | SER249 |
| B | HOH3102 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1006 |
| Chain | Residue |
| A | VAL247 |
| A | SER248 |
| A | HOH3003 |
| A | HOH3033 |
| A | HOH3288 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1007 |
| Chain | Residue |
| A | PRO346 |
| A | GLU347 |
| A | HIS348 |
| A | HOH3101 |
| A | HOH3149 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 13P B 2001 |
| Chain | Residue |
| B | LYS120 |
| B | LYS204 |
| B | ASN205 |
| B | THR264 |
| B | GLY268 |
| B | ARG269 |
| B | ASN270 |
| B | NAD3002 |
| B | HOH3012 |
| B | HOH3013 |
| B | HOH3161 |
| B | HOH3191 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 13P A 2002 |
| Chain | Residue |
| A | LYS120 |
| A | GLY149 |
| A | LYS204 |
| A | ASN205 |
| A | ASP260 |
| A | THR264 |
| A | GLY268 |
| A | ARG269 |
| A | ASN270 |
| A | NAD3001 |
| A | HOH3005 |
| A | HOH3037 |
| A | HOH3058 |
| A | HOH3136 |
| A | HOH3197 |
| site_id | BC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD A 3001 |
| Chain | Residue |
| A | SER11 |
| A | GLY12 |
| A | ASN13 |
| A | TRP14 |
| A | GLY15 |
| A | PHE41 |
| A | TYR63 |
| A | VAL92 |
| A | PRO94 |
| A | PHE97 |
| A | LEU118 |
| A | LYS120 |
| A | ASN151 |
| A | ILE152 |
| A | ALA153 |
| A | ARG269 |
| A | GLY294 |
| A | GLN295 |
| A | LYS296 |
| A | GLN298 |
| A | 13P2002 |
| A | HOH3026 |
| A | HOH3038 |
| A | HOH3054 |
| A | HOH3056 |
| A | HOH3058 |
| A | HOH3197 |
| site_id | BC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD B 3002 |
| Chain | Residue |
| B | VAL93 |
| B | PRO94 |
| B | PHE97 |
| B | LEU118 |
| B | ILE119 |
| B | LYS120 |
| B | ASN151 |
| B | ILE152 |
| B | ALA153 |
| B | ARG269 |
| B | GLY294 |
| B | GLN295 |
| B | LYS296 |
| B | GLN298 |
| B | 13P2001 |
| B | HOH3011 |
| B | HOH3013 |
| B | HOH3020 |
| B | HOH3023 |
| B | HOH3037 |
| B | HOH3120 |
| B | SER11 |
| B | GLY12 |
| B | ASN13 |
| B | TRP14 |
| B | GLY15 |
| B | PHE41 |
| B | TYR63 |
Functional Information from PROSITE/UniProt
| site_id | PS00957 |
| Number of Residues | 22 |
| Details | NAD_G3PDH NAD-dependent glycerol-3-phosphate dehydrogenase signature. GALKNVVAvGaGFcdGLgFGdN |
| Chain | Residue | Details |
| A | GLY201-ASN222 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16460752","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P13707","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O35077","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1evy |
| Chain | Residue | Details |
| A | LYS204 | |
| A | THR264 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1evy |
| Chain | Residue | Details |
| B | LYS204 | |
| B | THR264 |
