Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003723 | molecular_function | RNA binding |
A | 0003743 | molecular_function | translation initiation factor activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006413 | biological_process | translational initiation |
B | 0003723 | molecular_function | RNA binding |
B | 0003743 | molecular_function | translation initiation factor activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006413 | biological_process | translational initiation |
C | 0003723 | molecular_function | RNA binding |
C | 0003743 | molecular_function | translation initiation factor activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006413 | biological_process | translational initiation |
D | 0003723 | molecular_function | RNA binding |
D | 0003743 | molecular_function | translation initiation factor activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006413 | biological_process | translational initiation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | binding site for residue 7L2 A 301 |
Chain | Residue |
A | PHE48 |
A | TRP102 |
A | GLU103 |
A | ARG157 |
A | LYS159 |
A | LYS162 |
A | ARG186 |
A | LYS206 |
A | HOH403 |
A | HOH414 |
A | HOH419 |
A | ASN50 |
A | HOH429 |
A | HOH430 |
A | HOH452 |
A | HOH485 |
A | HOH521 |
A | ASP51 |
A | LYS52 |
A | LYS54 |
A | TRP56 |
A | GLN57 |
A | ASN59 |
A | MET101 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue GOL A 302 |
Chain | Residue |
A | ILE115 |
A | THR116 |
A | GLN121 |
A | HOH413 |
A | HOH442 |
site_id | AC3 |
Number of Residues | 23 |
Details | binding site for residue 7L2 B 301 |
Chain | Residue |
B | PHE48 |
B | ASN50 |
B | ASP51 |
B | LYS52 |
B | LYS54 |
B | TRP56 |
B | ASN59 |
B | MET101 |
B | TRP102 |
B | GLU103 |
B | ARG157 |
B | LYS162 |
B | ARG186 |
B | HOH418 |
B | HOH426 |
B | HOH429 |
B | HOH447 |
B | HOH454 |
B | HOH477 |
B | HOH478 |
B | HOH505 |
B | HOH525 |
B | HOH527 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL B 302 |
Chain | Residue |
B | ILE115 |
B | THR116 |
B | LEU117 |
B | GLN121 |
B | HOH442 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL B 303 |
Chain | Residue |
B | TRP46 |
B | GLN57 |
B | LEU60 |
B | GLU99 |
B | MET101 |
B | HOH512 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue 7L2 C 300 |
Chain | Residue |
C | LYS52 |
C | LYS54 |
C | TRP56 |
C | ASN59 |
C | MET101 |
C | TRP102 |
C | GLU103 |
C | ARG157 |
C | LYS162 |
site_id | AC7 |
Number of Residues | 9 |
Details | binding site for residue 7L2 D 300 |
Chain | Residue |
D | ASP51 |
D | LYS52 |
D | LYS54 |
D | TRP56 |
D | ASN59 |
D | MET101 |
D | TRP102 |
D | ARG157 |
D | LYS162 |
Functional Information from PROSITE/UniProt
site_id | PS00813 |
Number of Residues | 24 |
Details | IF4E Eukaryotic initiation factor 4E signature. DYslFKdgIePmWEDeknkrGGRW |
Chain | Residue | Details |
A | ASP90-TRP113 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | TRP56 | |
C | TRP102 | |
C | ARG157 | |
C | THR205 | |
D | TRP56 | |
D | TRP102 | |
D | ARG157 | |
D | THR205 | |
A | TRP102 | |
A | ARG157 | |
A | THR205 | |
B | TRP56 | |
B | TRP102 | |
B | ARG157 | |
B | THR205 | |
C | TRP56 | |
Chain | Residue | Details |
A | SER209 | |
B | SER209 | |
C | SER209 | |
D | SER209 | |