3FD5
Crystal structure of human selenophosphate synthetase 1 complex with AMPCP
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0016260 | biological_process | selenocysteine biosynthetic process |
A | 0016301 | molecular_function | kinase 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 | 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 | 0016260 | biological_process | selenocysteine biosynthetic process |
B | 0016301 | molecular_function | kinase 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 | 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 | 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 |