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 activity |
A | 0004032 | molecular_function | aldose reductase (NADPH) activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
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 activity |
B | 0004032 | molecular_function | aldose reductase (NADPH) activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
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 activity |
C | 0004032 | molecular_function | aldose reductase (NADPH) activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
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 activity |
D | 0004032 | molecular_function | aldose reductase (NADPH) activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
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 | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P15121 |
Chain | Residue | Details |
A | GLN48 | |
B | GLN48 | |
C | GLN48 | |
D | GLN48 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | ALA9 | |
B | ALA9 | |
C | ALA9 | |
D | ALA9 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | TRP110 | |
B | TRP110 | |
C | TRP110 | |
D | TRP110 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P15121 |
Chain | Residue | Details |
A | PRO210 | |
B | PRO210 | |
C | PRO210 | |
D | PRO210 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Lowers pKa of active site Tyr => ECO:0000250 |
Chain | Residue | Details |
A | LEU77 | |
B | LEU77 | |
C | LEU77 | |
D | LEU77 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:8281941 |
Chain | Residue | Details |
A | SER1 | |
B | SER1 | |
C | SER1 | |
D | SER1 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07943 |
Chain | Residue | Details |
A | HIS2 | |
B | HIS2 | |
C | HIS2 | |
D | HIS2 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P15121 |
Chain | Residue | Details |
A | PRO221 | |
A | SER262 | |
B | PRO221 | |
B | SER262 | |
C | PRO221 | |
C | SER262 | |
D | PRO221 | |
D | SER262 |
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 |