4ZDO
The crystal structure of T325S mutant of human SepSecS in complex with selenocysteine tRNA (tRNASec)
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 | 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 | 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 | 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 | 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 | 16 |
Details | binding site for residue PLR A 1001 |
Chain | Residue |
A | ARG75 |
A | TYR255 |
A | LYS284 |
A | PRO311 |
A | GLY312 |
A | ARG313 |
A | HOH1102 |
A | HOH1134 |
A | ALA143 |
A | THR144 |
A | GLY145 |
A | ILE170 |
A | GLN172 |
A | SER174 |
A | ASN252 |
A | ALA254 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue PO4 A 1002 |
Chain | Residue |
A | ARG97 |
A | SER98 |
A | GLN105 |
A | HOH1166 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue PLR B 1001 |
Chain | Residue |
B | ARG75 |
B | SER98 |
B | ALA143 |
B | THR144 |
B | GLY145 |
B | GLN172 |
B | SER174 |
B | CYS175 |
B | ASN252 |
B | ALA254 |
B | TYR255 |
B | LYS284 |
B | GLY312 |
B | ARG313 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue PO4 B 1002 |
Chain | Residue |
B | ARG97 |
B | SER98 |
B | GLN105 |
B | ARG313 |
B | HOH1101 |
B | HOH1152 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue PO4 C 1002 |
Chain | Residue |
C | ARG97 |
C | GLN105 |
C | HOH1113 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue PO4 D 1002 |
Chain | Residue |
D | ARG97 |
D | GLN105 |
D | ARG313 |
D | HOH1122 |
site_id | AC7 |
Number of Residues | 20 |
Details | binding site for Di-peptide PLR C 1001 and LYS C 284 |
Chain | Residue |
C | ARG75 |
C | SER98 |
C | ALA143 |
C | THR144 |
C | GLY145 |
C | ILE170 |
C | GLN172 |
C | SER174 |
C | ASN252 |
C | ALA254 |
C | TYR255 |
C | SER281 |
C | LEU282 |
C | ASP283 |
C | ASN285 |
C | PHE286 |
C | GLY312 |
C | ARG313 |
C | ILE440 |
C | HOH1122 |
site_id | AC8 |
Number of Residues | 22 |
Details | binding site for Di-peptide PLR D 1001 and LYS D 284 |
Chain | Residue |
D | GLU74 |
D | ARG75 |
D | SER98 |
D | ALA143 |
D | THR144 |
D | GLY145 |
D | ILE170 |
D | GLN172 |
D | SER174 |
D | ASN252 |
D | ALA254 |
D | TYR255 |
D | SER281 |
D | LEU282 |
D | ASP283 |
D | ASN285 |
D | PHE286 |
D | GLY312 |
D | ARG313 |
D | ILE440 |
D | HOH1117 |
D | HOH1137 |
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 |