4J7U
Crystal structure of human sepiapterin reductase in complex with sulfathiazole
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 |
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 | 0005739 | cellular_component | mitochondrion |
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 | 0005739 | cellular_component | mitochondrion |
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 | 29 |
Details | BINDING SITE FOR RESIDUE NAP A 801 |
Chain | Residue |
A | GLY11 |
A | ASP66 |
A | LEU67 |
A | ASN97 |
A | LEU123 |
A | ILE152 |
A | SER153 |
A | TYR167 |
A | LYS171 |
A | PRO195 |
A | GLY196 |
A | SER13 |
A | PRO197 |
A | LEU198 |
A | THR200 |
A | MET202 |
A | GLN203 |
A | YTZ802 |
A | HOH907 |
A | HOH918 |
A | HOH919 |
A | HOH921 |
A | ARG14 |
A | GLY15 |
A | PHE16 |
A | ALA38 |
A | ARG39 |
A | ASN40 |
A | ALA65 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE YTZ A 802 |
Chain | Residue |
A | SER154 |
A | LEU155 |
A | PHE161 |
A | TYR167 |
A | GLY196 |
A | PRO197 |
A | GLN203 |
A | NAP801 |
A | PEG806 |
A | HOH905 |
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 | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 804 |
Chain | Residue |
A | ARG59 |
D | ARG45 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG A 805 |
Chain | Residue |
A | ASP254 |
A | PEG806 |
A | HOH943 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG A 806 |
Chain | Residue |
A | GLY218 |
A | YTZ802 |
A | PEG805 |
A | HOH943 |
site_id | AC7 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAP B 801 |
Chain | Residue |
B | GLY11 |
B | SER13 |
B | ARG14 |
B | GLY15 |
B | PHE16 |
B | ARG39 |
B | ASN40 |
B | ALA65 |
B | ASP66 |
B | LEU67 |
B | ASN97 |
B | ALA98 |
B | ILE152 |
B | SER153 |
B | TYR167 |
B | LYS171 |
B | PRO195 |
B | GLY196 |
B | PRO197 |
B | LEU198 |
B | THR200 |
B | MET202 |
B | GLN203 |
B | YTZ802 |
B | HOH906 |
B | HOH918 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE YTZ B 802 |
Chain | Residue |
B | SER154 |
B | LEU155 |
B | PHE161 |
B | TRP164 |
B | TYR167 |
B | GLY196 |
B | PRO197 |
B | GLN203 |
B | NAP801 |
B | GOL805 |
B | HOH901 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 B 803 |
Chain | Residue |
B | ARG39 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG B 804 |
Chain | Residue |
B | ASP214 |
B | GOL805 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 805 |
Chain | Residue |
B | ASP254 |
B | YTZ802 |
B | PEG804 |
site_id | BC3 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAP C 801 |
Chain | Residue |
C | ALA65 |
C | ASP66 |
C | LEU67 |
C | ASN97 |
C | ALA98 |
C | LEU123 |
C | ILE152 |
C | SER153 |
C | TYR167 |
C | LYS171 |
C | PRO195 |
C | GLY196 |
C | PRO197 |
C | LEU198 |
C | THR200 |
C | MET202 |
C | GLN203 |
C | YTZ802 |
C | HOH901 |
C | HOH915 |
C | HOH917 |
C | HOH919 |
C | HOH942 |
C | GLY11 |
C | SER13 |
C | ARG14 |
C | GLY15 |
C | PHE16 |
C | ARG39 |
C | ASN40 |
site_id | BC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE YTZ C 802 |
Chain | Residue |
C | SER154 |
C | LEU155 |
C | CYS156 |
C | PHE161 |
C | TYR167 |
C | GLY196 |
C | PRO197 |
C | GLN203 |
C | NAP801 |
C | PEG805 |
C | HOH902 |
site_id | BC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 C 803 |
Chain | Residue |
C | ARG39 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 C 804 |
Chain | Residue |
A | ARG45 |
C | ARG59 |
site_id | BC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG C 805 |
Chain | Residue |
C | GLY218 |
C | YTZ802 |
site_id | BC8 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAP D 801 |
Chain | Residue |
D | GLY11 |
D | SER13 |
D | ARG14 |
D | GLY15 |
D | PHE16 |
D | ARG39 |
D | ASN40 |
D | ALA65 |
D | ASP66 |
D | LEU67 |
D | ASN97 |
D | ALA98 |
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 | YTZ802 |
site_id | BC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE YTZ D 802 |
Chain | Residue |
D | SER154 |
D | LEU155 |
D | TYR167 |
D | GLY196 |
D | PRO197 |
D | GLN203 |
D | NAP801 |
D | HOH914 |
site_id | CC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 D 803 |
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 |