4Z3K
Human sepiapterin reductase in complex with the cofactor NADP+ and the trypthophan metabolite xanthurenic acid
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 NAP A 801 |
Chain | Residue |
A | GLY11 |
A | ASP66 |
A | LEU67 |
A | ASN97 |
A | ALA98 |
A | GLY99 |
A | LEU123 |
A | ILE152 |
A | SER153 |
A | TYR167 |
A | LYS171 |
A | SER13 |
A | PRO195 |
A | GLY196 |
A | PRO197 |
A | LEU198 |
A | THR200 |
A | ASP201 |
A | MET202 |
A | GLN203 |
A | 4KL802 |
A | HOH907 |
A | ARG14 |
A | HOH910 |
A | HOH917 |
A | HOH930 |
A | GLY15 |
A | PHE16 |
A | ALA38 |
A | ARG39 |
A | ASN40 |
A | ALA65 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue 4KL A 802 |
Chain | Residue |
A | SER154 |
A | LEU155 |
A | TRP164 |
A | TYR167 |
A | GLN203 |
A | LEU219 |
A | NAP801 |
A | HOH901 |
A | HOH908 |
A | HOH915 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue SO4 A 803 |
Chain | Residue |
A | ARG39 |
site_id | AC4 |
Number of Residues | 29 |
Details | binding site for residue NAP 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 | ALA98 |
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 | 4KL302 |
B | HOH406 |
B | HOH410 |
site_id | AC5 |
Number of Residues | 11 |
Details | binding site for residue 4KL B 302 |
Chain | Residue |
B | SER154 |
B | LEU155 |
B | TRP164 |
B | TYR167 |
B | PRO197 |
B | GLN203 |
B | NAP301 |
B | HOH401 |
B | HOH402 |
B | HOH403 |
B | HOH418 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue SO4 B 303 |
Chain | Residue |
C | LYS87 |
C | GLY88 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 304 |
Chain | Residue |
B | ARG39 |
B | HOH413 |
B | HOH427 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue EDO B 305 |
Chain | Residue |
B | LYS217 |
B | GLN220 |
site_id | AC9 |
Number of Residues | 29 |
Details | binding site for residue NAP C 301 |
Chain | Residue |
C | ASP66 |
C | LEU67 |
C | ASN97 |
C | ILE152 |
C | SER153 |
C | TYR167 |
C | LYS171 |
C | PRO195 |
C | GLY196 |
C | PRO197 |
C | LEU198 |
C | THR200 |
C | ASP201 |
C | MET202 |
C | GLN203 |
C | 4KL302 |
C | HOH409 |
C | HOH413 |
C | HOH415 |
C | HOH431 |
C | GLY11 |
C | SER13 |
C | ARG14 |
C | GLY15 |
C | PHE16 |
C | ALA38 |
C | ARG39 |
C | ASN40 |
C | ALA65 |
site_id | AD1 |
Number of Residues | 12 |
Details | binding site for residue 4KL C 302 |
Chain | Residue |
C | SER154 |
C | LEU155 |
C | TRP164 |
C | TYR167 |
C | PRO197 |
C | GLN203 |
C | LEU219 |
C | NAP301 |
C | SO4304 |
C | HOH401 |
C | HOH405 |
C | HOH410 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue SO4 C 303 |
Chain | Residue |
C | ARG39 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue SO4 C 304 |
Chain | Residue |
C | CYS156 |
C | PHE161 |
C | TRP164 |
C | MET215 |
C | 4KL302 |
C | HOH401 |
site_id | AD4 |
Number of Residues | 30 |
Details | binding site for residue NAP 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 | GLY99 |
D | LEU123 |
D | ILE152 |
D | SER153 |
D | TYR167 |
D | LYS171 |
D | PRO195 |
D | GLY196 |
D | PRO197 |
D | LEU198 |
D | THR200 |
D | MET202 |
D | GLN203 |
D | 4KL302 |
D | HOH410 |
D | HOH427 |
D | HOH429 |
site_id | AD5 |
Number of Residues | 12 |
Details | binding site for residue 4KL D 302 |
Chain | Residue |
D | SER154 |
D | LEU155 |
D | TRP164 |
D | TYR167 |
D | PRO197 |
D | GLN203 |
D | NAP301 |
D | SO4303 |
D | HOH401 |
D | HOH403 |
D | HOH408 |
D | HOH422 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue SO4 D 303 |
Chain | Residue |
D | CYS156 |
D | PHE161 |
D | TRP164 |
D | MET215 |
D | 4KL302 |
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 |