3FD6
Crystal structure of human selenophosphate synthetase 1 complex with ADP and phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004756 | molecular_function | selenide, water dikinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0016020 | cellular_component | membrane |
| A | 0016260 | biological_process | selenocysteine biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0031965 | cellular_component | nuclear membrane |
| A | 0036211 | biological_process | protein modification process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004756 | molecular_function | selenide, water dikinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0016020 | cellular_component | membrane |
| B | 0016260 | biological_process | selenocysteine biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0031965 | cellular_component | nuclear membrane |
| B | 0036211 | biological_process | protein modification process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ADP A 393 |
| Chain | Residue |
| A | LYS32 |
| A | PHE269 |
| A | PO4394 |
| A | MG395 |
| A | MG396 |
| A | MG397 |
| A | NA398 |
| A | HOH445 |
| A | HOH447 |
| A | HOH476 |
| A | HOH480 |
| A | LEU38 |
| B | MET124 |
| B | VAL159 |
| B | GLY161 |
| B | GLY162 |
| B | GLN163 |
| B | THR164 |
| B | HOH618 |
| A | LEU42 |
| A | ILE66 |
| A | GLY67 |
| A | MET68 |
| A | ASP69 |
| A | ASP110 |
| A | THR267 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 394 |
| Chain | Residue |
| A | LYS32 |
| A | ASP87 |
| A | ASN106 |
| A | THR267 |
| A | GLY268 |
| A | ADP393 |
| A | MG396 |
| A | MG397 |
| A | HOH426 |
| A | HOH427 |
| B | GLN163 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 395 |
| Chain | Residue |
| A | ASP69 |
| A | ASP110 |
| A | ASP265 |
| A | ADP393 |
| A | HOH399 |
| A | HOH425 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 396 |
| Chain | Residue |
| A | ASP110 |
| A | ADP393 |
| A | PO4394 |
| A | MG397 |
| A | HOH399 |
| A | HOH426 |
| A | HOH427 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 398 |
| Chain | Residue |
| A | ASP69 |
| A | THR85 |
| A | ADP393 |
| B | HOH429 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 397 |
| Chain | Residue |
| A | GLN163 |
| A | HOH421 |
| B | ASP87 |
| B | ADP393 |
| B | PO4394 |
| B | MG396 |
| B | HOH430 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 397 |
| Chain | Residue |
| A | ADP393 |
| A | PO4394 |
| A | MG396 |
| A | HOH427 |
| A | HOH447 |
| B | GLN163 |
| site_id | AC8 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ADP B 393 |
| Chain | Residue |
| A | MET124 |
| A | LEU126 |
| A | GLY161 |
| A | GLY162 |
| A | GLN163 |
| A | THR164 |
| A | HOH421 |
| B | LYS32 |
| B | LEU42 |
| B | GLY67 |
| B | MET68 |
| B | ASP69 |
| B | ASP110 |
| B | PHE269 |
| B | PO4394 |
| B | MG395 |
| B | MG396 |
| B | MG397 |
| B | NA398 |
| B | HOH430 |
| B | HOH451 |
| B | HOH453 |
| B | HOH456 |
| B | HOH560 |
| B | HOH822 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PO4 B 394 |
| Chain | Residue |
| B | MG396 |
| B | MG397 |
| B | HOH399 |
| B | HOH423 |
| B | HOH660 |
| A | GLN163 |
| B | LYS32 |
| B | ASP87 |
| B | ASN106 |
| B | THR267 |
| B | GLY268 |
| B | ADP393 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 395 |
| Chain | Residue |
| B | ASP69 |
| B | ASP110 |
| B | ASP265 |
| B | ADP393 |
| B | HOH399 |
| B | HOH424 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 396 |
| Chain | Residue |
| B | ASP110 |
| B | ADP393 |
| B | PO4394 |
| B | MG397 |
| B | HOH399 |
| B | HOH423 |
| B | HOH430 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 398 |
| Chain | Residue |
| B | ASP69 |
| B | THR85 |
| B | ASP110 |
| B | ADP393 |
| B | HOH422 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255 |
| Chain | Residue | Details |
| A | CYS31 | |
| B | CYS31 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:19477186, ECO:0007744|PDB:3FD5, ECO:0007744|PDB:3FD6 |
| Chain | Residue | Details |
| A | LYS32 | |
| A | GLY67 | |
| B | LYS32 | |
| B | GLY67 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19477186, ECO:0007744|PDB:3FD6 |
| Chain | Residue | Details |
| A | ASP69 | |
| A | ASP110 | |
| A | ASP265 | |
| B | ASP69 | |
| B | ASP110 | |
| B | ASP265 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:19477186, ECO:0007744|PDB:3FD5 |
| Chain | Residue | Details |
| A | ASP87 | |
| B | ASP87 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19477186, ECO:0007744|PDB:3FD5, ECO:0007744|PDB:3FD6 |
| Chain | Residue | Details |
| A | GLY161 | |
| B | GLY161 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity => ECO:0000250|UniProtKB:P16456 |
| Chain | Residue | Details |
| A | LYS32 | |
| B | LYS32 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330 |
| Chain | Residue | Details |
| A | SER2 | |
| B | SER2 |
