1EFU
ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003723 | molecular_function | RNA binding |
A | 0003746 | molecular_function | translation elongation factor activity |
A | 0003924 | molecular_function | GTPase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005525 | molecular_function | GTP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005886 | cellular_component | plasma membrane |
A | 0006412 | biological_process | translation |
A | 0006414 | biological_process | translational elongation |
A | 0032045 | cellular_component | guanyl-nucleotide exchange factor complex |
A | 0046677 | biological_process | response to antibiotic |
A | 0097216 | molecular_function | guanosine tetraphosphate binding |
B | 0003746 | molecular_function | translation elongation factor activity |
B | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006412 | biological_process | translation |
B | 0006414 | biological_process | translational elongation |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016020 | cellular_component | membrane |
B | 0032045 | cellular_component | guanyl-nucleotide exchange factor complex |
C | 0003723 | molecular_function | RNA binding |
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 | 0005886 | cellular_component | plasma membrane |
C | 0006412 | biological_process | translation |
C | 0006414 | biological_process | translational elongation |
C | 0032045 | cellular_component | guanyl-nucleotide exchange factor complex |
C | 0046677 | biological_process | response to antibiotic |
C | 0097216 | molecular_function | guanosine tetraphosphate binding |
D | 0003746 | molecular_function | translation elongation factor activity |
D | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006412 | biological_process | translation |
D | 0006414 | biological_process | translational elongation |
D | 0008270 | molecular_function | zinc ion binding |
D | 0016020 | cellular_component | membrane |
D | 0032045 | cellular_component | guanyl-nucleotide exchange factor 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. DNapeEKaRGITIntS |
Chain | Residue | Details |
A | ASP50-SER65 |
site_id | PS01126 |
Number of Residues | 16 |
Details | EF_TS_1 Elongation factor Ts signature 1. LRerTGaGMmDcKKAL |
Chain | Residue | Details |
B | LEU11-LEU26 |
site_id | PS01127 |
Number of Residues | 11 |
Details | EF_TS_2 Elongation factor Ts signature 2. EVNCQTDFVAK |
Chain | Residue | Details |
B | GLU74-LYS84 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS19 | |
A | CYS81 | |
A | LYS136 | |
C | HIS19 | |
C | CYS81 | |
C | LYS136 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
A | THR38 | |
C | PRO295 | |
A | ALA177 | |
A | GLU249 | |
A | SER253 | |
A | PRO295 | |
C | THR38 | |
C | ALA177 | |
C | GLU249 | |
C | SER253 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:2022614, ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545 |
Chain | Residue | Details |
A | ALA57 | |
C | ALA57 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
A | ASP314 | |
C | ASP314 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000305|PubMed:19150849, ECO:0000305|PubMed:24141193, ECO:0000305|PubMed:8416965 |
Chain | Residue | Details |
A | VAL383 | |
C | VAL383 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
A | ASP21 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
C | ASP21 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
A | HIS84 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ksj |
Chain | Residue | Details |
C | HIS84 |