3FD5
Crystal structure of human selenophosphate synthetase 1 complex with AMPCP
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 | 0005694 | cellular_component | chromosome |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006351 | biological_process | DNA-templated transcription |
| 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 | 0045454 | biological_process | cell redox homeostasis |
| 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 | 0005694 | cellular_component | chromosome |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006351 | biological_process | DNA-templated transcription |
| 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 | 0045454 | biological_process | cell redox homeostasis |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE AP2 A 393 |
| Chain | Residue |
| A | LYS32 |
| A | HIS274 |
| A | PO4394 |
| A | MG395 |
| A | MG396 |
| A | MG397 |
| A | K398 |
| A | HOH413 |
| A | HOH415 |
| A | HOH718 |
| A | HOH810 |
| A | LEU42 |
| B | MET124 |
| B | LEU126 |
| B | VAL159 |
| B | GLY161 |
| B | GLY162 |
| B | GLN163 |
| B | THR164 |
| B | HOH511 |
| A | GLY67 |
| A | MET68 |
| A | ASP69 |
| A | ASP87 |
| A | ASP110 |
| A | THR267 |
| A | PHE269 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 394 |
| Chain | Residue |
| A | LYS32 |
| A | ASP87 |
| A | THR267 |
| A | GLY268 |
| A | HIS274 |
| A | AP2393 |
| A | MG396 |
| A | MG397 |
| A | HOH611 |
| A | HOH752 |
| 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 | AP2393 |
| A | HOH399 |
| A | HOH718 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 396 |
| Chain | Residue |
| A | ASP87 |
| A | ASP110 |
| A | AP2393 |
| A | PO4394 |
| A | MG397 |
| A | HOH399 |
| A | HOH828 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 397 |
| Chain | Residue |
| A | ASP87 |
| A | AP2393 |
| A | PO4394 |
| A | MG396 |
| A | HOH658 |
| B | GLN163 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 398 |
| Chain | Residue |
| A | ASP69 |
| A | THR85 |
| A | ASP110 |
| A | AP2393 |
| A | HOH658 |
| A | HOH659 |
| site_id | AC7 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE AP2 B 393 |
| Chain | Residue |
| A | MET124 |
| A | LEU126 |
| A | VAL159 |
| A | GLY161 |
| A | GLY162 |
| A | GLN163 |
| A | THR164 |
| A | HOH460 |
| A | HOH661 |
| B | LYS32 |
| B | LEU38 |
| B | LEU42 |
| B | LEU45 |
| B | GLY67 |
| B | MET68 |
| B | ASP69 |
| B | ASP87 |
| B | ASP110 |
| B | PHE269 |
| B | HIS274 |
| B | PO4394 |
| B | MG395 |
| B | MG396 |
| B | MG397 |
| B | K398 |
| B | HOH414 |
| B | HOH417 |
| B | HOH543 |
| B | HOH590 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PO4 B 394 |
| Chain | Residue |
| B | MG396 |
| B | MG397 |
| B | HOH399 |
| B | HOH416 |
| B | HOH423 |
| B | HOH597 |
| B | HOH719 |
| A | GLN163 |
| B | LYS32 |
| B | ASP87 |
| B | THR267 |
| B | GLY268 |
| B | HIS274 |
| B | AP2393 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 395 |
| Chain | Residue |
| B | ASP69 |
| B | ASP110 |
| B | ASP265 |
| B | AP2393 |
| B | MG396 |
| B | HOH399 |
| B | HOH590 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MG B 396 |
| Chain | Residue |
| B | ASP87 |
| B | ASP110 |
| B | AP2393 |
| B | PO4394 |
| B | MG395 |
| B | MG397 |
| B | K398 |
| B | HOH399 |
| B | HOH719 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE K B 398 |
| Chain | Residue |
| B | ASP69 |
| B | THR85 |
| B | THR86 |
| B | ASP87 |
| B | ASP110 |
| B | AP2393 |
| B | MG396 |
| B | HOH417 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 397 |
| Chain | Residue |
| A | GLN163 |
| A | HOH661 |
| B | ASP87 |
| B | AP2393 |
| B | PO4394 |
| B | MG396 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"19477186","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FD5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FD6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19477186","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FD6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"19477186","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FD5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19477186","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FD5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FD6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P16456","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
