3AVY
Structure of viral RNA polymerase complex 6
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0001172 | biological_process | RNA-templated transcription |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003746 | molecular_function | translation elongation factor activity |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0003968 | molecular_function | RNA-directed RNA polymerase 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 | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019079 | biological_process | viral genome replication |
| A | 0032045 | cellular_component | guanyl-nucleotide exchange factor complex |
| A | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
| A | 0039694 | biological_process | viral RNA genome replication |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CH1 A 2501 |
| Chain | Residue |
| A | LYS908 |
| A | ASP1053 |
| A | CA3001 |
| A | CA3002 |
| G | U2013 |
| T | G2104 |
| T | A2105 |
| A | ARG914 |
| A | ASP968 |
| A | LEU969 |
| A | SER970 |
| A | ALA972 |
| A | SER973 |
| A | MET1017 |
| A | GLU1026 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 3001 |
| Chain | Residue |
| A | ASP968 |
| A | LEU969 |
| A | ASP1053 |
| A | CH12501 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 3002 |
| Chain | Residue |
| A | ASP968 |
| A | ASP1053 |
| A | ASP1054 |
| A | CH12501 |
| G | U2013 |
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 | ASP335-SER350 |
| 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 | 7 |
| Details | Region: {"description":"G1","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Region: {"description":"G3","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Region: {"description":"G4","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Region: {"description":"G5","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00118","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Region: {"description":"Involved in Mg(2+) ion dislocation from EF-Tu"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 132 |
| Details | Domain: {"description":"RdRp catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00539","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 3 |
| 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 |
