1N0V
Crystal structure of elongation factor 2
Functional Information from GO Data
Chain | GOid | namespace | contents |
C | 0003746 | molecular_function | translation elongation factor activity |
C | 0003924 | molecular_function | GTPase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005525 | molecular_function | GTP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006412 | biological_process | translation |
C | 0006414 | biological_process | translational elongation |
C | 0016787 | molecular_function | hydrolase activity |
C | 0019843 | molecular_function | rRNA binding |
C | 0042802 | molecular_function | identical protein binding |
C | 0043022 | molecular_function | ribosome binding |
C | 0045901 | biological_process | positive regulation of translational elongation |
C | 0051087 | molecular_function | protein-folding chaperone binding |
C | 1990145 | biological_process | maintenance of translational fidelity |
C | 1990904 | cellular_component | ribonucleoprotein complex |
D | 0003746 | molecular_function | translation elongation factor activity |
D | 0003924 | molecular_function | GTPase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005525 | molecular_function | GTP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006412 | biological_process | translation |
D | 0006414 | biological_process | translational elongation |
D | 0016787 | molecular_function | hydrolase activity |
D | 0019843 | molecular_function | rRNA binding |
D | 0042802 | molecular_function | identical protein binding |
D | 0043022 | molecular_function | ribosome binding |
D | 0045901 | biological_process | positive regulation of translational elongation |
D | 0051087 | molecular_function | protein-folding chaperone binding |
D | 1990145 | biological_process | maintenance of translational fidelity |
D | 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 |
C | ASP58-THR73 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:15316019, ECO:0000305|PubMed:17082187, ECO:0007744|PDB:1U2R, ECO:0007744|PDB:2NPF |
Chain | Residue | Details |
C | ALA26 | |
D | ALA26 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:15316019, ECO:0000305|PubMed:17082187, ECO:0007744|PDB:1U2R, ECO:0007744|PDB:2E1R, ECO:0007744|PDB:2NPF |
Chain | Residue | Details |
C | ASN158 | |
C | SER213 | |
D | ASN158 | |
D | SER213 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; by EFM3; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354 |
Chain | Residue | Details |
C | LYS509 | |
D | LYS509 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
C | SER579 | |
D | SER579 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; by EFM2; alternate => ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25086354 |
Chain | Residue | Details |
C | LYS613 | |
D | LYS613 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Diphthamide => ECO:0000269|PubMed:15316019, ECO:0000269|PubMed:16950777, ECO:0000269|PubMed:721806 |
Chain | Residue | Details |
C | HIS699 | |
D | HIS699 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
C | THR713 | |
C | THR763 | |
D | THR713 | |
D | THR763 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 |
Chain | Residue | Details |
C | LYS841 | |
D | LYS841 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
C | ASP29 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
D | ASP29 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
C | HIS108 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
D | HIS108 |