3MMP
Structure of the Qb replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins
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 | 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 | 0032045 | cellular_component | guanyl-nucleotide exchange factor complex |
A | 0046677 | biological_process | response to antibiotic |
A | 0097216 | molecular_function | guanosine tetraphosphate 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 | 0032045 | cellular_component | guanyl-nucleotide exchange factor complex |
C | 0046677 | biological_process | response to antibiotic |
C | 0097216 | molecular_function | guanosine tetraphosphate binding |
F | 0000166 | molecular_function | nucleotide binding |
F | 0001172 | biological_process | RNA-templated transcription |
F | 0003723 | molecular_function | RNA binding |
F | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
F | 0005515 | molecular_function | protein binding |
F | 0019079 | biological_process | viral genome replication |
F | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
F | 0039694 | biological_process | viral RNA genome replication |
F | 0046872 | molecular_function | metal ion binding |
G | 0000166 | molecular_function | nucleotide binding |
G | 0001172 | biological_process | RNA-templated transcription |
G | 0003723 | molecular_function | RNA binding |
G | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
G | 0005515 | molecular_function | protein binding |
G | 0019079 | biological_process | viral genome replication |
G | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
G | 0039694 | biological_process | viral RNA genome replication |
G | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PXN A 1394 |
Chain | Residue |
A | HOH741 |
A | HOH887 |
A | ARG1262 |
G | PRO143 |
G | MET148 |
G | TYR186 |
G | ALA189 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PXN C 1394 |
Chain | Residue |
F | MET148 |
F | TYR186 |
C | ARG1262 |
F | PRO143 |
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 | ASP1050-SER1065 |
site_id | PS01126 |
Number of Residues | 16 |
Details | EF_TS_1 Elongation factor Ts signature 1. LRerTGaGMmDcKKAL |
Chain | Residue | Details |
A | LEU11-LEU26 |
site_id | PS01127 |
Number of Residues | 11 |
Details | EF_TS_2 Elongation factor Ts signature 2. EVNCQTDFVAK |
Chain | Residue | Details |
A | GLU74-LYS84 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418 |
Chain | Residue | Details |
G | ASP274 | |
G | ASP359 | |
G | ASP360 | |
F | ASP274 | |
F | ASP359 | |
F | ASP360 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545 |
Chain | Residue | Details |
A | SER1001 | |
C | SER1001 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
A | LYS1037 | |
C | LYS1294 | |
A | LYS1176 | |
A | LYS1248 | |
A | LYS1252 | |
A | LYS1294 | |
C | LYS1037 | |
C | LYS1176 | |
C | LYS1248 | |
C | LYS1252 |
site_id | SWS_FT_FI4 |
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 | LYS1056 | |
C | LYS1056 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
A | LYS1313 | |
C | LYS1313 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000305|PubMed:19150849, ECO:0000305|PubMed:24141193, ECO:0000305|PubMed:8416965 |
Chain | Residue | Details |
A | THR1382 | |
C | THR1382 |