6I6T
SEPIAPTERIN REDUCTASE IN COMPLEX WITH COMPOUND 5
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0070062 | cellular_component | extracellular exosome |
| 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 | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| 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 | 26 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human sepiapterin reductase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P18297","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by CaMK2; in vitro","evidences":[{"source":"PubMed","id":"11825621","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
