3HL2
The crystal structure of the human SepSecS-tRNASec complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0001514 | biological_process | selenocysteine incorporation |
| A | 0001717 | biological_process | conversion of seryl-tRNAsec to selenocys-tRNAsec |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006412 | biological_process | translation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0098621 | molecular_function | O-phosphoseryl-tRNA(Sec) selenium transferase activity |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0001514 | biological_process | selenocysteine incorporation |
| B | 0001717 | biological_process | conversion of seryl-tRNAsec to selenocys-tRNAsec |
| B | 0003723 | molecular_function | RNA binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006412 | biological_process | translation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0098621 | molecular_function | O-phosphoseryl-tRNA(Sec) selenium transferase activity |
| C | 0000049 | molecular_function | tRNA binding |
| C | 0001514 | biological_process | selenocysteine incorporation |
| C | 0001717 | biological_process | conversion of seryl-tRNAsec to selenocys-tRNAsec |
| C | 0003723 | molecular_function | RNA binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006412 | biological_process | translation |
| C | 0016740 | molecular_function | transferase activity |
| C | 0098621 | molecular_function | O-phosphoseryl-tRNA(Sec) selenium transferase activity |
| D | 0000049 | molecular_function | tRNA binding |
| D | 0001514 | biological_process | selenocysteine incorporation |
| D | 0001717 | biological_process | conversion of seryl-tRNAsec to selenocys-tRNAsec |
| D | 0003723 | molecular_function | RNA binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006412 | biological_process | translation |
| D | 0016740 | molecular_function | transferase activity |
| D | 0098621 | molecular_function | O-phosphoseryl-tRNA(Sec) selenium transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLR A 1001 |
| Chain | Residue |
| A | GLU74 |
| A | ASN252 |
| A | ALA254 |
| A | TYR255 |
| A | LYS284 |
| A | GLY312 |
| A | ARG313 |
| A | HOH525 |
| A | HOH564 |
| A | ARG75 |
| A | ALA143 |
| A | THR144 |
| A | GLY145 |
| A | ILE170 |
| A | GLN172 |
| A | SER174 |
| A | CYS175 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE TS6 A 3001 |
| Chain | Residue |
| A | ARG97 |
| A | SER98 |
| A | GLN105 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE TS6 A 3002 |
| Chain | Residue |
| A | ARG199 |
| A | HIS368 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLR B 1001 |
| Chain | Residue |
| B | ARG75 |
| B | ALA143 |
| B | THR144 |
| B | GLY145 |
| B | ILE170 |
| B | GLN172 |
| B | SER174 |
| B | ASN252 |
| B | ALA254 |
| B | TYR255 |
| B | LYS284 |
| B | PRO311 |
| B | GLY312 |
| B | ARG313 |
| B | HOH570 |
| B | SEP2001 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SEP B 2001 |
| Chain | Residue |
| B | GLU74 |
| B | ARG75 |
| B | ARG97 |
| B | SER98 |
| B | GLY99 |
| B | GLN105 |
| B | GLN172 |
| B | LYS173 |
| B | PHE227 |
| B | LYS284 |
| B | ARG313 |
| B | HOH570 |
| B | PLR1001 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SEP B 2002 |
| Chain | Residue |
| B | ARG199 |
| B | ARG234 |
| B | HIS368 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLR C 1001 |
| Chain | Residue |
| C | ARG75 |
| C | ALA143 |
| C | THR144 |
| C | GLY145 |
| C | ILE170 |
| C | GLN172 |
| C | SER174 |
| C | CYS175 |
| C | ASN252 |
| C | ALA254 |
| C | TYR255 |
| C | LYS284 |
| C | GLY312 |
| C | ARG313 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE TS6 C 3001 |
| Chain | Residue |
| C | ARG97 |
| C | SER98 |
| C | GLN105 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLR D 1001 |
| Chain | Residue |
| D | ARG75 |
| D | ALA143 |
| D | THR144 |
| D | GLY145 |
| D | GLN172 |
| D | SER174 |
| D | CYS175 |
| D | ASN252 |
| D | ALA254 |
| D | TYR255 |
| D | LYS284 |
| D | GLY312 |
| D | ARG313 |
| D | SEP2001 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SEP D 2001 |
| Chain | Residue |
| D | GLU74 |
| D | ARG75 |
| D | ARG97 |
| D | SER98 |
| D | GLY99 |
| D | GLN105 |
| D | GLN172 |
| D | LYS173 |
| D | LYS284 |
| D | ARG313 |
| D | PLR1001 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SEP D 2002 |
| Chain | Residue |
| D | HOH535 |
| D | ARG199 |
| D | ARG234 |
| D | HIS368 |
Functional Information from PROSITE/UniProt
| site_id | PS00435 |
| Number of Residues | 11 |
| Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. DIIKLAGVHTV |
| Chain | Residue | Details |
| A | ASP124-VAL134 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19608919 |
| Chain | Residue | Details |
| A | ARG75 | |
| B | ARG97 | |
| B | SER98 | |
| B | GLN105 | |
| B | ARG271 | |
| B | ARG313 | |
| B | ARG398 | |
| B | LYS463 | |
| C | ARG75 | |
| C | ARG97 | |
| C | SER98 | |
| A | ARG97 | |
| C | GLN105 | |
| C | ARG271 | |
| C | ARG313 | |
| C | ARG398 | |
| C | LYS463 | |
| D | ARG75 | |
| D | ARG97 | |
| D | SER98 | |
| D | GLN105 | |
| D | ARG271 | |
| A | SER98 | |
| D | ARG313 | |
| D | ARG398 | |
| D | LYS463 | |
| A | GLN105 | |
| A | ARG271 | |
| A | ARG313 | |
| A | ARG398 | |
| A | LYS463 | |
| B | ARG75 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate => ECO:0000250|UniProtKB:Q6P6M7 |
| Chain | Residue | Details |
| A | GLU74 | |
| B | GLU74 | |
| C | GLU74 | |
| D | GLU74 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER14 | |
| B | SER14 | |
| C | SER14 | |
| D | SER14 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:19608919 |
| Chain | Residue | Details |
| A | LYS284 | |
| B | LYS284 | |
| C | LYS284 | |
| D | LYS284 |
