3DNY
Fitting of the eEF2 crystal structure into the cryo-EM density map of the eEF2.80S.AlF4-.GDP complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| T | 0000166 | molecular_function | nucleotide binding |
| T | 0003723 | molecular_function | RNA binding |
| T | 0003746 | molecular_function | translation elongation factor activity |
| T | 0003924 | molecular_function | GTPase activity |
| T | 0005515 | molecular_function | protein binding |
| T | 0005525 | molecular_function | GTP binding |
| T | 0005737 | cellular_component | cytoplasm |
| T | 0005829 | cellular_component | cytosol |
| T | 0006412 | biological_process | translation |
| T | 0006414 | biological_process | translational elongation |
| T | 0016787 | molecular_function | hydrolase activity |
| T | 0019843 | molecular_function | rRNA binding |
| T | 0042802 | molecular_function | identical protein binding |
| T | 0043022 | molecular_function | ribosome binding |
| T | 0045901 | biological_process | positive regulation of translational elongation |
| T | 0051087 | molecular_function | protein-folding chaperone binding |
| T | 1990145 | biological_process | maintenance of translational fidelity |
| T | 1990904 | cellular_component | ribonucleoprotein complex |
Functional Information from PROSITE/UniProt
| site_id | PS00301 |
| Number of Residues | 16 |
| Details | G_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DTrkdEQeRGITIksT |
| Chain | Residue | Details |
| T | ASP58-THR73 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15316019","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17082187","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1U2R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NPF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15316019","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17082187","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1U2R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2E1R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NPF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Diphthamide","evidences":[{"source":"PubMed","id":"15316019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16950777","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"721806","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| T | ASP29 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| T | HIS108 |
