6I6P
SEPIAPTERIN REDUCTASE IN COMPLEX WITH COMPOUND 3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004757 | molecular_function | sepiapterin reductase (NADP+) activity |
| 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 | 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 | LEU126 |
| A | ILE155 |
| A | SER156 |
| A | TYR170 |
| A | LYS174 |
| A | PRO198 |
| A | SER16 |
| A | GLY199 |
| A | PRO200 |
| A | LEU201 |
| A | THR203 |
| A | ASP204 |
| A | MET205 |
| A | GLN206 |
| A | H4T302 |
| A | EDO303 |
| A | HOH417 |
| A | ARG17 |
| A | HOH431 |
| A | HOH444 |
| A | HOH464 |
| A | HOH467 |
| A | HOH477 |
| A | HOH518 |
| A | HOH522 |
| A | GLY18 |
| A | PHE19 |
| A | ALA41 |
| A | ARG42 |
| A | ASN43 |
| A | ALA68 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue H4T A 302 |
| Chain | Residue |
| A | SER157 |
| A | CYS159 |
| A | PHE164 |
| A | TYR170 |
| A | PRO200 |
| A | MET205 |
| A | GLN206 |
| A | MET218 |
| A | NAP301 |
| A | HOH440 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | ARG17 |
| A | ASP204 |
| A | NAP301 |
| site_id | AC4 |
| 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 | LEU126 |
| B | ILE155 |
| B | SER156 |
| B | TYR170 |
| B | LYS174 |
| B | PRO198 |
| B | GLY199 |
| B | PRO200 |
| B | LEU201 |
| B | THR203 |
| B | ASP204 |
| B | MET205 |
| B | GLN206 |
| B | H4T302 |
| B | EDO304 |
| B | HOH408 |
| B | HOH418 |
| B | HOH419 |
| B | HOH442 |
| B | HOH451 |
| B | HOH464 |
| B | HOH498 |
| B | HOH536 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue H4T B 302 |
| Chain | Residue |
| A | TYR-3 |
| B | SER157 |
| B | LEU158 |
| B | PHE164 |
| B | TYR170 |
| B | MET205 |
| B | GLN206 |
| B | MET218 |
| B | NAP301 |
| B | HOH423 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | ALA125 |
| B | THR129 |
| B | SER130 |
| A | ASN121 |
| B | LEU70 |
| B | GLU73 |
| B | LEU76 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| B | ARG17 |
| B | ASP204 |
| B | NAP301 |
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 | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","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":"UniProtKB","id":"P18297","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by CaMK2; in vitro","evidences":[{"source":"PubMed","id":"11825621","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
