6I6T
SEPIAPTERIN REDUCTASE IN COMPLEX WITH COMPOUND 5
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 PDB Data
site_id | AC1 |
Number of Residues | 36 |
Details | binding site for residue NAP A 301 |
Chain | Residue |
A | GLY14 |
A | ASP69 |
A | LEU70 |
A | ASN100 |
A | ALA101 |
A | GLY102 |
A | LEU126 |
A | ILE155 |
A | SER156 |
A | TYR170 |
A | LYS174 |
A | SER16 |
A | PRO198 |
A | GLY199 |
A | PRO200 |
A | LEU201 |
A | THR203 |
A | MET205 |
A | GLN206 |
A | H5B302 |
A | EDO304 |
A | HOH401 |
A | ARG17 |
A | HOH425 |
A | HOH426 |
A | HOH434 |
A | HOH445 |
A | HOH449 |
A | HOH454 |
A | HOH466 |
A | GLY18 |
A | PHE19 |
A | ALA41 |
A | ARG42 |
A | ASN43 |
A | ALA68 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue H5B A 302 |
Chain | Residue |
A | SER157 |
A | LEU158 |
A | TRP167 |
A | LEU222 |
A | LEU225 |
A | NAP301 |
A | EDO304 |
A | HOH408 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue H5B A 303 |
Chain | Residue |
A | LEU83 |
A | ARG84 |
A | LEU86 |
A | PRO87 |
A | ARG88 |
A | PHE142 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | LEU104 |
A | TRP167 |
A | TYR170 |
A | GLN206 |
A | NAP301 |
A | H5B302 |
site_id | AC5 |
Number of Residues | 36 |
Details | binding site for residue NAP B 301 |
Chain | Residue |
B | GLY14 |
B | SER16 |
B | ARG17 |
B | GLY18 |
B | PHE19 |
B | ALA41 |
B | ARG42 |
B | ASN43 |
B | ALA68 |
B | ASP69 |
B | LEU70 |
B | ASN100 |
B | ALA101 |
B | GLY102 |
B | LEU126 |
B | ILE155 |
B | SER156 |
B | TYR170 |
B | LYS174 |
B | PRO198 |
B | GLY199 |
B | PRO200 |
B | LEU201 |
B | THR203 |
B | MET205 |
B | GLN206 |
B | H5B302 |
B | EDO304 |
B | HOH406 |
B | HOH419 |
B | HOH422 |
B | HOH440 |
B | HOH446 |
B | HOH457 |
B | HOH460 |
B | HOH471 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue H5B B 302 |
Chain | Residue |
B | SER157 |
B | LEU158 |
B | TRP167 |
B | LEU222 |
B | NAP301 |
B | EDO304 |
B | HOH410 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue H5B B 303 |
Chain | Residue |
B | VAL9 |
B | LEU83 |
B | ARG84 |
B | LEU86 |
B | PRO87 |
B | ARG88 |
B | ALA141 |
B | PHE142 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
B | TYR170 |
B | GLN206 |
B | NAP301 |
B | H5B302 |
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 |