1Z6Z
Crystal Structure of Human Sepiapterin Reductase in complex with NADP+
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 |
| C | 0004757 | molecular_function | sepiapterin reductase (NADP+) activity |
| 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 | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0050661 | molecular_function | NADP binding |
| C | 0070062 | cellular_component | extracellular exosome |
| D | 0004757 | molecular_function | sepiapterin reductase (NADP+) activity |
| 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 | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0050661 | molecular_function | NADP binding |
| D | 0070062 | cellular_component | extracellular exosome |
| E | 0004757 | molecular_function | sepiapterin reductase (NADP+) activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005739 | cellular_component | mitochondrion |
| E | 0005829 | cellular_component | cytosol |
| E | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| E | 0006809 | biological_process | nitric oxide biosynthetic process |
| E | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0050661 | molecular_function | NADP binding |
| E | 0070062 | cellular_component | extracellular exosome |
| F | 0004757 | molecular_function | sepiapterin reductase (NADP+) activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005739 | cellular_component | mitochondrion |
| F | 0005829 | cellular_component | cytosol |
| F | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| F | 0006809 | biological_process | nitric oxide biosynthetic process |
| F | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0050661 | molecular_function | NADP binding |
| F | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| A | LYS87 |
| A | GLY88 |
| A | LEU89 |
| C | ARG45 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 401 |
| Chain | Residue |
| A | ARG39 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL C 402 |
| Chain | Residue |
| C | ARG39 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL D 403 |
| Chain | Residue |
| D | ARG39 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL C 405 |
| Chain | Residue |
| C | GLY88 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 406 |
| Chain | Residue |
| C | TYR167 |
| C | NAP803 |
| B | TYR-4 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 407 |
| Chain | Residue |
| A | SER154 |
| A | TYR167 |
| A | NAP801 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 408 |
| Chain | Residue |
| B | SER154 |
| B | TYR167 |
| B | NAP802 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 409 |
| Chain | Residue |
| D | SER154 |
| D | TYR167 |
| D | NAP804 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL E 410 |
| Chain | Residue |
| E | SER154 |
| E | TYR167 |
| E | NAP805 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL F 411 |
| Chain | Residue |
| F | SER154 |
| F | TYR167 |
| F | NAP806 |
| site_id | BC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP A 801 |
| Chain | Residue |
| A | GLY11 |
| A | SER13 |
| A | ARG14 |
| A | GLY15 |
| A | PHE16 |
| A | ALA38 |
| A | ARG39 |
| A | ASN40 |
| A | ALA65 |
| A | ASP66 |
| A | LEU67 |
| A | ASN97 |
| A | LEU123 |
| A | ILE152 |
| A | SER153 |
| A | TYR167 |
| A | LYS171 |
| A | PRO195 |
| A | GLY196 |
| A | PRO197 |
| A | LEU198 |
| A | THR200 |
| A | MET202 |
| A | GLN203 |
| A | CL407 |
| A | HOH802 |
| A | HOH808 |
| A | HOH831 |
| A | HOH843 |
| A | HOH851 |
| A | HOH856 |
| site_id | BC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAP B 802 |
| 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 | LEU123 |
| B | ILE152 |
| B | SER153 |
| B | TYR167 |
| B | LYS171 |
| B | PRO195 |
| B | GLY196 |
| B | PRO197 |
| B | LEU198 |
| B | THR200 |
| B | MET202 |
| B | GLN203 |
| B | CL408 |
| B | HOH826 |
| B | HOH829 |
| site_id | BC5 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAP C 803 |
| Chain | Residue |
| C | TYR167 |
| C | LYS171 |
| C | PRO195 |
| C | GLY196 |
| C | PRO197 |
| C | LEU198 |
| C | THR200 |
| C | MET202 |
| C | GLN203 |
| C | CL406 |
| C | HOH808 |
| C | HOH836 |
| C | HOH837 |
| C | HOH857 |
| C | HOH863 |
| C | GLY11 |
| C | SER13 |
| C | ARG14 |
| C | GLY15 |
| C | PHE16 |
| C | ARG39 |
| C | ASN40 |
| C | ALA65 |
| C | ASP66 |
| C | LEU67 |
| C | ASN97 |
| C | ALA98 |
| C | LEU123 |
| C | ILE152 |
| C | SER153 |
| site_id | BC6 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAP D 804 |
| 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 | LEU123 |
| D | ILE152 |
| D | SER153 |
| D | TYR167 |
| D | LYS171 |
| D | PRO195 |
| D | GLY196 |
| D | PRO197 |
| D | LEU198 |
| D | THR200 |
| D | MET202 |
| D | GLN203 |
| D | CL409 |
| D | HOH808 |
| D | HOH811 |
| D | HOH817 |
| D | HOH837 |
| site_id | BC7 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAP E 805 |
| Chain | Residue |
| E | GLY11 |
| E | SER13 |
| E | ARG14 |
| E | GLY15 |
| E | PHE16 |
| E | ARG39 |
| E | ASN40 |
| E | ALA65 |
| E | ASP66 |
| E | LEU67 |
| E | ASN97 |
| E | LEU123 |
| E | ILE152 |
| E | SER153 |
| E | TYR167 |
| E | LYS171 |
| E | PRO195 |
| E | GLY196 |
| E | PRO197 |
| E | LEU198 |
| E | THR200 |
| E | MET202 |
| E | GLN203 |
| E | CL410 |
| site_id | BC8 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAP F 806 |
| Chain | Residue |
| F | GLY11 |
| F | SER13 |
| F | ARG14 |
| F | GLY15 |
| F | PHE16 |
| F | ARG39 |
| F | ASN40 |
| F | ALA65 |
| F | ASP66 |
| F | LEU67 |
| F | ASN97 |
| F | LEU123 |
| F | ILE152 |
| F | SER153 |
| F | TYR167 |
| F | LYS171 |
| F | PRO195 |
| F | GLY196 |
| F | PRO197 |
| F | LEU198 |
| F | THR200 |
| F | MET202 |
| F | GLN203 |
| F | CL411 |
| F | HOH815 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 78 |
| 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 | 30 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P18297","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine; by CaMK2; in vitro","evidences":[{"source":"PubMed","id":"11825621","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | SER154 | |
| A | TYR167 | |
| A | ASN124 | |
| A | LYS171 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| D | TRP164 | |
| D | LYS171 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| E | TRP164 | |
| E | LYS171 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| F | TRP164 | |
| F | LYS171 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | TYR167 | |
| A | LYS171 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| B | TYR167 | |
| B | LYS171 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| C | TYR167 | |
| C | LYS171 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| D | TYR167 | |
| D | LYS171 |
| site_id | CSA17 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| E | TYR167 | |
| E | LYS171 |
| site_id | CSA18 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| F | TYR167 | |
| F | LYS171 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| B | SER154 | |
| B | TYR167 | |
| B | ASN124 | |
| B | LYS171 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| C | SER154 | |
| C | TYR167 | |
| C | ASN124 | |
| C | LYS171 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| D | SER154 | |
| D | TYR167 | |
| D | ASN124 | |
| D | LYS171 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| E | SER154 | |
| E | TYR167 | |
| E | ASN124 | |
| E | LYS171 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| F | SER154 | |
| F | TYR167 | |
| F | ASN124 | |
| F | LYS171 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | TRP164 | |
| A | LYS171 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| B | TRP164 | |
| B | LYS171 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| C | TRP164 | |
| C | LYS171 |






