5IZL
The crystal structure of human eEFSec in complex with GDPCP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0001514 | biological_process | selenocysteine incorporation |
| A | 0003746 | molecular_function | translation elongation factor activity |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006412 | biological_process | translation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0035368 | molecular_function | selenocysteine insertion sequence binding |
| A | 0043021 | molecular_function | ribonucleoprotein complex binding |
| A | 1990904 | cellular_component | ribonucleoprotein complex |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0001514 | biological_process | selenocysteine incorporation |
| B | 0003746 | molecular_function | translation elongation factor activity |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006412 | biological_process | translation |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0035368 | molecular_function | selenocysteine insertion sequence binding |
| B | 0043021 | molecular_function | ribonucleoprotein complex binding |
| B | 1990904 | cellular_component | ribonucleoprotein complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 1001 |
| Chain | Residue |
| A | THR21 |
| A | THR48 |
| A | GCP1002 |
| A | HOH1104 |
| A | HOH1105 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | binding site for residue GCP A 1002 |
| Chain | Residue |
| A | LYS20 |
| A | THR21 |
| A | ALA22 |
| A | GLU44 |
| A | ILE47 |
| A | THR48 |
| A | GLY95 |
| A | ASN146 |
| A | LYS147 |
| A | ASP149 |
| A | LEU150 |
| A | ALA186 |
| A | LYS187 |
| A | PRO188 |
| A | PRO191 |
| A | MG1001 |
| A | HOH1104 |
| A | HOH1105 |
| A | HOH1110 |
| A | ILE16 |
| A | ASP17 |
| A | SER18 |
| A | GLY19 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 1001 |
| Chain | Residue |
| B | THR21 |
| B | GLY46 |
| B | THR48 |
| B | GCP1002 |
| B | HOH1106 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | binding site for residue GCP B 1002 |
| Chain | Residue |
| B | ILE16 |
| B | ASP17 |
| B | SER18 |
| B | GLY19 |
| B | LYS20 |
| B | THR21 |
| B | ALA22 |
| B | ILE47 |
| B | THR48 |
| B | ASN146 |
| B | LYS147 |
| B | ASP149 |
| B | LEU150 |
| B | ALA185 |
| B | ALA186 |
| B | LYS187 |
| B | PRO191 |
| B | MG1001 |
| B | HOH1106 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:27708257 |
| Chain | Residue | Details |
| A | GLY19 | |
| A | ALA22 | |
| A | ASP149 | |
| A | LYS187 | |
| B | GLY19 | |
| B | ALA22 | |
| B | ASP149 | |
| B | LYS187 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27708257, ECO:0007744|PDB:5IZL |
| Chain | Residue | Details |
| A | THR21 | |
| A | THR48 | |
| A | ASP92 | |
| B | THR21 | |
| B | THR48 | |
| B | ASP92 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER537 | |
| B | SER537 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9JHW4 |
| Chain | Residue | Details |
| A | THR545 | |
| B | THR545 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q9JHW4 |
| Chain | Residue | Details |
| A | ARG556 | |
| B | ARG556 |
