1DLA
NOVEL NADPH-BINDING DOMAIN REVEALED BY THE CRYSTAL STRUCTURE OF ALDOSE REDUCTASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001523 | biological_process | retinoid metabolic process |
| A | 0001758 | molecular_function | retinal dehydrogenase (NAD+) activity |
| A | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006060 | biological_process | sorbitol metabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006693 | biological_process | prostaglandin metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0036130 | molecular_function | prostaglandin H2 endoperoxidase reductase activity |
| A | 0042572 | biological_process | retinol metabolic process |
| A | 0047655 | molecular_function | allyl-alcohol dehydrogenase activity |
| A | 0047956 | molecular_function | glycerol dehydrogenase (NADP+) activity |
| A | 0052650 | molecular_function | all-trans-retinol dehydrogenase (NADP+) activity |
| B | 0001523 | biological_process | retinoid metabolic process |
| B | 0001758 | molecular_function | retinal dehydrogenase (NAD+) activity |
| B | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006060 | biological_process | sorbitol metabolic process |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006693 | biological_process | prostaglandin metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0036130 | molecular_function | prostaglandin H2 endoperoxidase reductase activity |
| B | 0042572 | biological_process | retinol metabolic process |
| B | 0047655 | molecular_function | allyl-alcohol dehydrogenase activity |
| B | 0047956 | molecular_function | glycerol dehydrogenase (NADP+) activity |
| B | 0052650 | molecular_function | all-trans-retinol dehydrogenase (NADP+) activity |
| C | 0001523 | biological_process | retinoid metabolic process |
| C | 0001758 | molecular_function | retinal dehydrogenase (NAD+) activity |
| C | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006060 | biological_process | sorbitol metabolic process |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0006693 | biological_process | prostaglandin metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0036130 | molecular_function | prostaglandin H2 endoperoxidase reductase activity |
| C | 0042572 | biological_process | retinol metabolic process |
| C | 0047655 | molecular_function | allyl-alcohol dehydrogenase activity |
| C | 0047956 | molecular_function | glycerol dehydrogenase (NADP+) activity |
| C | 0052650 | molecular_function | all-trans-retinol dehydrogenase (NADP+) activity |
| D | 0001523 | biological_process | retinoid metabolic process |
| D | 0001758 | molecular_function | retinal dehydrogenase (NAD+) activity |
| D | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006060 | biological_process | sorbitol metabolic process |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0006693 | biological_process | prostaglandin metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0036130 | molecular_function | prostaglandin H2 endoperoxidase reductase activity |
| D | 0042572 | biological_process | retinol metabolic process |
| D | 0047655 | molecular_function | allyl-alcohol dehydrogenase activity |
| D | 0047956 | molecular_function | glycerol dehydrogenase (NADP+) activity |
| D | 0052650 | molecular_function | all-trans-retinol dehydrogenase (NADP+) activity |
Functional Information from PROSITE/UniProt
| site_id | PS00062 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MeelvdeglVKAIGVSNF |
| Chain | Residue | Details |
| A | MET143-PHE160 |
| site_id | PS00063 |
| Number of Residues | 16 |
| Details | ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVTpeRIaENfQV |
| Chain | Residue | Details |
| A | ILE259-VAL274 |
| site_id | PS00798 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAhvyqnEneVG |
| Chain | Residue | Details |
| A | GLY37-GLY54 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P15121","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| 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 | 4 |
| Details | Site: {"description":"Lowers pKa of active site Tyr","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07943","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P15121","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 62 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P15121","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | HIS109 | |
| A | ASP42 | |
| A | LYS76 | |
| A | TYR47 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| B | HIS109 | |
| B | ASP42 | |
| B | LYS76 | |
| B | TYR47 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| C | HIS109 | |
| C | ASP42 | |
| C | LYS76 | |
| C | TYR47 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| D | HIS109 | |
| D | ASP42 | |
| D | LYS76 | |
| D | TYR47 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | TYR47 | |
| A | LYS76 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| B | TYR47 | |
| B | LYS76 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| C | TYR47 | |
| C | LYS76 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| D | TYR47 | |
| D | LYS76 |
