4R71
Structure of the Qbeta holoenzyme complex in the P1211 crystal form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003746 | molecular_function | translation elongation factor activity |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006412 | biological_process | translation |
| A | 0006414 | biological_process | translational elongation |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0032045 | cellular_component | guanyl-nucleotide exchange factor complex |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097216 | molecular_function | guanosine tetraphosphate binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0001172 | biological_process | RNA-templated transcription |
| B | 0003723 | molecular_function | RNA binding |
| B | 0003968 | molecular_function | RNA-directed RNA polymerase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0019079 | biological_process | viral genome replication |
| B | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
| B | 0039694 | biological_process | viral RNA genome replication |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003723 | molecular_function | RNA binding |
| C | 0003746 | molecular_function | translation elongation factor activity |
| C | 0003924 | molecular_function | GTPase activity |
| C | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005525 | molecular_function | GTP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006412 | biological_process | translation |
| C | 0006414 | biological_process | translational elongation |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016020 | cellular_component | membrane |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0032045 | cellular_component | guanyl-nucleotide exchange factor complex |
| C | 0046677 | biological_process | response to antibiotic |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0097216 | molecular_function | guanosine tetraphosphate binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0001172 | biological_process | RNA-templated transcription |
| D | 0003723 | molecular_function | RNA binding |
| D | 0003968 | molecular_function | RNA-directed RNA polymerase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016779 | molecular_function | nucleotidyltransferase activity |
| D | 0019079 | biological_process | viral genome replication |
| D | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
| D | 0039694 | biological_process | viral RNA genome replication |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0003676 | molecular_function | nucleic acid binding |
| F | 0003676 | molecular_function | nucleic acid binding |
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 | ASP1051-SER1066 |
| site_id | PS01126 |
| Number of Residues | 16 |
| Details | EF_TS_1 Elongation factor Ts signature 1. LRerTGaGMmDcKKAL |
| Chain | Residue | Details |
| A | LEU12-LEU27 |
| site_id | PS01127 |
| Number of Residues | 11 |
| Details | EF_TS_2 Elongation factor Ts signature 2. EVNCQTDFVAK |
| Chain | Residue | Details |
| A | GLU75-LYS85 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Region: {"description":"Involved in Mg(2+) ion dislocation from EF-Tu","evidences":[{"source":"HAMAP-Rule","id":"MF_00050","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Region: {"description":"G1","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Region: {"description":"G3","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Region: {"description":"G4","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Region: {"description":"G5","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 28 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00118","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"6997043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7021545","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 10 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19150849","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24141193","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8416965","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 264 |
| Details | Domain: {"description":"RdRp catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00539","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20798060","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22245970","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22884418","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
