3U0O
The crystal structure of selenophosphate synthetase from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004756 | molecular_function | selenide, water dikinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0016260 | biological_process | selenocysteine biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070329 | biological_process | tRNA seleno-modification |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004756 | molecular_function | selenide, water dikinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0016260 | biological_process | selenocysteine biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070329 | biological_process | tRNA seleno-modification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | ASP51 |
| A | ASP91 |
| A | ASP227 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | ASP91 |
| B | ASP227 |
| B | THR229 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00625 |
| Chain | Residue | Details |
| A | CYS17 | |
| B | CYS17 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: in other chain => ECO:0000250|UniProtKB:P49903, ECO:0000255|HAMAP-Rule:MF_00625 |
| Chain | Residue | Details |
| A | LYS20 | |
| A | THR48 | |
| A | ASP68 | |
| B | LYS20 | |
| B | THR48 | |
| B | ASP68 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00625, ECO:0000269|PubMed:22081394, ECO:0007744|PDB:3U0O |
| Chain | Residue | Details |
| A | ASP51 | |
| A | ASP91 | |
| A | ASP227 | |
| B | ASP51 | |
| B | ASP91 | |
| B | ASP227 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P49903, ECO:0000255|HAMAP-Rule:MF_00625 |
| Chain | Residue | Details |
| A | GLY139 | |
| B | GLY139 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00625, ECO:0000269|PubMed:8262938 |
| Chain | Residue | Details |
| A | LYS20 | |
| B | LYS20 |
