7DSF
The Crystal Structure of human SPR from Biortus.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004033 | molecular_function | aldo-keto reductase (NADPH) activity |
| A | 0004757 | molecular_function | sepiapterin reductase (NADP+) activity |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| A | 0006809 | biological_process | nitric oxide biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0004033 | molecular_function | aldo-keto reductase (NADPH) activity |
| B | 0004757 | molecular_function | sepiapterin reductase (NADP+) activity |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| B | 0006809 | biological_process | nitric oxide biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0050661 | molecular_function | NADP binding |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|Ref.14 |
| Chain | Residue | Details |
| A | GLY14 | |
| A | ARG42 | |
| A | ASP69 | |
| A | LEU201 | |
| B | GLY14 | |
| B | ARG42 | |
| B | ASP69 | |
| B | LEU201 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | SER157 | |
| B | ASP257 | |
| A | TYR170 | |
| A | LYS174 | |
| A | GLY199 | |
| A | ASP257 | |
| B | SER157 | |
| B | TYR170 | |
| B | LYS174 | |
| B | GLY199 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P18297 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P18297 |
| Chain | Residue | Details |
| A | SER32 | |
| B | SER32 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER103 | |
| B | SER103 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by CaMK2; in vitro => ECO:0000269|PubMed:11825621 |
| Chain | Residue | Details |
| A | SER213 | |
| B | SER213 |
