Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006457 | biological_process | protein folding |
| A | 0061770 | molecular_function | translation elongation factor binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006457 | biological_process | protein folding |
| B | 0061770 | molecular_function | translation elongation factor binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006457 | biological_process | protein folding |
| C | 0061770 | molecular_function | translation elongation factor binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006457 | biological_process | protein folding |
| D | 0061770 | molecular_function | translation elongation factor binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 401 |
| Chain | Residue |
| A | LYS225 |
| A | VAL226 |
| A | HOH572 |
| D | ASN26 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 401 |
| Chain | Residue |
| B | ASN26 |
| C | LYS225 |
| C | VAL226 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 401 |
| Chain | Residue |
| D | ASN83 |
| C | LYS194 |
| D | LYS79 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N-acetylthreonine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
