4XWY
Crystal structure of human sepiapterin reductase in complex with an N-acetylserotinin analogue
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 | 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 | 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 |
| C | 0004033 | molecular_function | aldo-keto reductase (NADPH) activity |
| C | 0004757 | molecular_function | sepiapterin reductase (NADP+) activity |
| C | 0005654 | cellular_component | nucleoplasm |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| C | 0006809 | biological_process | nitric oxide biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0050661 | molecular_function | NADP binding |
| C | 0070062 | cellular_component | extracellular exosome |
| D | 0004033 | molecular_function | aldo-keto reductase (NADPH) activity |
| D | 0004757 | molecular_function | sepiapterin reductase (NADP+) activity |
| D | 0005654 | cellular_component | nucleoplasm |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| D | 0006809 | biological_process | nitric oxide biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0050661 | molecular_function | NADP binding |
| D | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | binding site for residue NDP A 801 |
| Chain | Residue |
| A | GLY11 |
| A | LEU67 |
| A | ASN97 |
| A | LEU123 |
| A | ILE152 |
| A | SER153 |
| A | TYR167 |
| A | LYS171 |
| A | PRO195 |
| A | GLY196 |
| A | PRO197 |
| A | SER13 |
| A | LEU198 |
| A | THR200 |
| A | MET202 |
| A | GLN203 |
| A | 43O802 |
| A | HOH922 |
| A | HOH924 |
| A | HOH927 |
| A | HOH950 |
| A | HOH951 |
| A | ARG14 |
| A | HOH963 |
| A | HOH964 |
| A | HOH967 |
| A | GLY15 |
| A | PHE16 |
| A | ARG39 |
| A | ASN40 |
| A | ALA65 |
| A | ASP66 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue 43O A 802 |
| Chain | Residue |
| A | SER154 |
| A | CYS156 |
| A | TRP164 |
| A | TYR167 |
| A | ALA194 |
| A | GLY196 |
| A | PRO197 |
| A | MET202 |
| A | ASP254 |
| A | NDP801 |
| A | HOH952 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 803 |
| Chain | Residue |
| A | ARG14 |
| A | GLY15 |
| A | HOH951 |
| B | LYS87 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 804 |
| Chain | Residue |
| A | ARG39 |
| A | HOH922 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 805 |
| Chain | Residue |
| A | LYS87 |
| A | GLY88 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 806 |
| Chain | Residue |
| B | ARG59 |
| B | VAL60 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | binding site for residue NDP B 301 |
| Chain | Residue |
| B | GLY11 |
| B | SER13 |
| B | ARG14 |
| B | GLY15 |
| B | PHE16 |
| B | ALA38 |
| B | ARG39 |
| B | ASN40 |
| B | ALA65 |
| B | ASP66 |
| B | LEU67 |
| B | ASN97 |
| B | GLY99 |
| B | LEU123 |
| B | ILE152 |
| B | SER153 |
| B | TYR167 |
| B | LYS171 |
| B | PRO195 |
| B | GLY196 |
| B | PRO197 |
| B | LEU198 |
| B | THR200 |
| B | MET202 |
| B | GLN203 |
| B | 43O302 |
| B | HOH403 |
| B | HOH411 |
| B | HOH424 |
| B | HOH441 |
| B | HOH467 |
| B | HOH468 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue 43O B 302 |
| Chain | Residue |
| B | SER154 |
| B | CYS156 |
| B | TRP164 |
| B | TYR167 |
| B | ALA194 |
| B | GLY196 |
| B | PRO197 |
| B | MET202 |
| B | ASP254 |
| B | NDP301 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 303 |
| Chain | Residue |
| B | LYS87 |
| B | GLY88 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 304 |
| Chain | Residue |
| B | LYS248 |
| B | SER249 |
| B | ARG189 |
| B | PHE247 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 305 |
| Chain | Residue |
| B | ARG39 |
| B | HOH424 |
| site_id | AD3 |
| Number of Residues | 35 |
| Details | binding site for residue NDP C 301 |
| Chain | Residue |
| C | GLY11 |
| C | SER13 |
| C | ARG14 |
| C | GLY15 |
| C | PHE16 |
| C | ALA38 |
| C | ARG39 |
| C | ASN40 |
| C | ALA65 |
| C | ASP66 |
| C | LEU67 |
| C | ASN97 |
| C | ALA98 |
| C | LEU123 |
| C | ILE152 |
| C | SER153 |
| C | SER154 |
| C | TYR167 |
| C | LYS171 |
| C | PRO195 |
| C | GLY196 |
| C | PRO197 |
| C | LEU198 |
| C | THR200 |
| C | MET202 |
| C | GLN203 |
| C | 43O302 |
| C | HOH409 |
| C | HOH437 |
| C | HOH440 |
| C | HOH446 |
| C | HOH448 |
| C | HOH455 |
| C | HOH469 |
| C | HOH470 |
| site_id | AD4 |
| Number of Residues | 11 |
| Details | binding site for residue 43O C 302 |
| Chain | Residue |
| C | SER154 |
| C | LEU155 |
| C | CYS156 |
| C | TRP164 |
| C | TYR167 |
| C | ALA194 |
| C | GLY196 |
| C | PRO197 |
| C | GLN203 |
| C | ASP254 |
| C | NDP301 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 303 |
| Chain | Residue |
| C | ARG39 |
| C | HOH434 |
| C | HOH446 |
| site_id | AD6 |
| Number of Residues | 33 |
| Details | binding site for residue NDP D 301 |
| Chain | Residue |
| D | GLY11 |
| D | SER13 |
| D | ARG14 |
| D | GLY15 |
| D | PHE16 |
| D | ALA38 |
| D | ARG39 |
| D | ASN40 |
| D | ALA65 |
| D | ASP66 |
| D | LEU67 |
| D | ASN97 |
| D | ALA98 |
| D | LEU123 |
| D | ILE152 |
| D | SER153 |
| D | SER154 |
| D | TYR167 |
| D | LYS171 |
| D | PRO195 |
| D | GLY196 |
| D | PRO197 |
| D | LEU198 |
| D | THR200 |
| D | ASP201 |
| D | MET202 |
| D | GLN203 |
| D | 43O302 |
| D | HOH412 |
| D | HOH426 |
| D | HOH427 |
| D | HOH437 |
| D | HOH438 |
| site_id | AD7 |
| Number of Residues | 10 |
| Details | binding site for residue 43O D 302 |
| Chain | Residue |
| D | SER154 |
| D | LEU155 |
| D | CYS156 |
| D | TRP164 |
| D | TYR167 |
| D | ALA194 |
| D | GLY196 |
| D | PRO197 |
| D | ASP254 |
| D | NDP301 |
| site_id | AD8 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 D 303 |
| Chain | Residue |
| D | ARG39 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|Ref.14 |
| Chain | Residue | Details |
| A | GLY11 | |
| C | ARG39 | |
| C | ASP66 | |
| C | LEU198 | |
| D | GLY11 | |
| D | ARG39 | |
| D | ASP66 | |
| D | LEU198 | |
| A | ARG39 | |
| A | ASP66 | |
| A | LEU198 | |
| B | GLY11 | |
| B | ARG39 | |
| B | ASP66 | |
| B | LEU198 | |
| C | GLY11 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | SER154 | |
| B | ASP254 | |
| C | SER154 | |
| C | TYR167 | |
| C | LYS171 | |
| C | GLY196 | |
| C | ASP254 | |
| D | SER154 | |
| D | TYR167 | |
| D | LYS171 | |
| D | GLY196 | |
| A | TYR167 | |
| D | ASP254 | |
| A | LYS171 | |
| A | GLY196 | |
| A | ASP254 | |
| B | SER154 | |
| B | TYR167 | |
| B | LYS171 | |
| B | GLY196 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P18297 |
| Chain | Residue | Details |
| A | MET-2 | |
| B | MET-2 | |
| C | MET-2 | |
| D | MET-2 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P18297 |
| Chain | Residue | Details |
| A | SER29 | |
| B | SER29 | |
| C | SER29 | |
| D | SER29 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER100 | |
| B | SER100 | |
| C | SER100 | |
| D | SER100 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by CaMK2; in vitro => ECO:0000269|PubMed:11825621 |
| Chain | Residue | Details |
| A | SER210 | |
| B | SER210 | |
| C | SER210 | |
| D | SER210 |
