5O8W
CRYSTAL STRUCTURE ANALYSIS OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000329 | cellular_component | fungal-type vacuole membrane |
A | 0001933 | biological_process | negative regulation of protein phosphorylation |
A | 0003746 | molecular_function | translation elongation factor activity |
A | 0003779 | molecular_function | actin binding |
A | 0003924 | molecular_function | GTPase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005525 | molecular_function | GTP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005829 | cellular_component | cytosol |
A | 0005840 | cellular_component | ribosome |
A | 0005853 | cellular_component | eukaryotic translation elongation factor 1 complex |
A | 0005856 | cellular_component | cytoskeleton |
A | 0006409 | biological_process | tRNA export from nucleus |
A | 0006412 | biological_process | translation |
A | 0006414 | biological_process | translational elongation |
A | 0006417 | biological_process | regulation of translation |
A | 0006469 | biological_process | negative regulation of protein kinase activity |
A | 0019003 | molecular_function | GDP binding |
A | 0019901 | molecular_function | protein kinase binding |
A | 0034198 | biological_process | cellular response to amino acid starvation |
A | 0043022 | molecular_function | ribosome binding |
A | 0051015 | molecular_function | actin filament binding |
A | 0051017 | biological_process | actin filament bundle assembly |
A | 1904408 | molecular_function | melatonin binding |
B | 0003746 | molecular_function | translation elongation factor activity |
B | 0005853 | cellular_component | eukaryotic translation elongation factor 1 complex |
B | 0006414 | biological_process | translational elongation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue GLN A 501 |
Chain | Residue |
A | GLU45 |
A | GLU48 |
A | ASN339 |
A | LEU374 |
A | HOH603 |
A | HOH613 |
A | HOH621 |
A | HOH701 |
A | HOH730 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue PGE A 502 |
Chain | Residue |
A | GLY273 |
A | GLU286 |
A | LEU385 |
A | GLU386 |
A | HOH833 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue PGE A 503 |
Chain | Residue |
A | LYS384 |
A | LEU385 |
A | ASP387 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue PGE B 1301 |
Chain | Residue |
A | ARG96 |
A | ARG428 |
A | HOH829 |
B | ASP1176 |
B | ASP1177 |
B | LYS1178 |
B | VAL1179 |
B | SER1180 |
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. DKlkaEReRGITIdiA |
Chain | Residue | Details |
A | ASP61-ALA76 |
site_id | PS00825 |
Number of Residues | 12 |
Details | EF1BD_2 Elongation factor 1 beta/beta'/delta chain signature 2. VQStDIaAMQKL |
Chain | Residue | Details |
B | VAL1195-LEU1206 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY14 | |
A | ASP91 | |
A | ASN153 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Not modified |
Chain | Residue | Details |
A | GLU298 | |
A | GLU372 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N,N,N-trimethylglycine; by EFM7 => ECO:0000269|PubMed:26545399 |
Chain | Residue | Details |
A | GLY2 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; by EFM7; alternate => ECO:0000269|PubMed:26545399 |
Chain | Residue | Details |
A | LYS3 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358 |
Chain | Residue | Details |
A | SER18 | |
A | SER163 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; by EFM1 => ECO:0000269|PubMed:22522802, ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:8476932 |
Chain | Residue | Details |
A | MLZ30 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:17287358 |
Chain | Residue | Details |
A | THR72 | |
A | THR82 | |
A | THR430 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N6,N6,N6-trimethyllysine; by EFM5 => ECO:0000269|PubMed:22522802, ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25446118, ECO:0000269|PubMed:8476932 |
Chain | Residue | Details |
A | M3L79 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956 |
Chain | Residue | Details |
A | THR259 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | SER289 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; by EFM4; alternate => ECO:0000269|PubMed:24517342 |
Chain | Residue | Details |
A | LYS316 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; by EFM6 => ECO:0000269|PubMed:22522802, ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:26115316, ECO:0000269|PubMed:8476932 |
Chain | Residue | Details |
A | LYS390 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
Chain | Residue | Details |
A | SER414 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Lysine methyl ester => ECO:0000269|PubMed:10973948 |
Chain | Residue | Details |
A | LYS458 |
site_id | SWS_FT_FI15 |
Number of Residues | 7 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 |
Chain | Residue | Details |
A | LYS224 | |
A | LYS242 | |
A | LYS253 | |
A | LYS271 | |
A | LYS393 | |
A | LYS437 |