8QHC
Cryo-EM structure of SidH from Legionella pneumophila in complex with LubX
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0000209 | biological_process | protein polyubiquitination |
| D | 0004842 | molecular_function | ubiquitin-protein transferase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| D | 0016567 | biological_process | protein ubiquitination |
| D | 0016740 | molecular_function | transferase activity |
| D | 0043161 | biological_process | proteasome-mediated ubiquitin-dependent protein catabolic process |
| D | 0043657 | cellular_component | host cell |
| D | 0045862 | biological_process | positive regulation of proteolysis |
| D | 0051087 | molecular_function | protein-folding chaperone binding |
| D | 0061630 | molecular_function | ubiquitin protein ligase activity |
| D | 0071218 | biological_process | cellular response to misfolded protein |
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 |
| C | ASP51-SER66 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: |
| Chain | Residue | Details |
| C | GLY19 | |
| C | ASP81 | |
| C | ASN136 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545 |
| Chain | Residue | Details |
| C | SER2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122 |
| Chain | Residue | Details |
| C | LYS38 | |
| C | LYS177 | |
| C | LYS249 | |
| C | LYS253 | |
| C | LYS295 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| 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 |
| C | LYS57 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 |
| Chain | Residue | Details |
| C | LYS314 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000305|PubMed:19150849, ECO:0000305|PubMed:24141193, ECO:0000305|PubMed:8416965 |
| Chain | Residue | Details |
| C | THR383 |
