7OYG
Dimeric form of SARS-CoV-2 RNA-dependent RNA polymerase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003723 | molecular_function | RNA binding |
A | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006351 | biological_process | DNA-templated transcription |
A | 0039694 | biological_process | viral RNA genome replication |
B | 0004197 | molecular_function | cysteine-type endopeptidase activity |
B | 0008242 | molecular_function | omega peptidase activity |
B | 0016740 | molecular_function | transferase activity |
C | 0004197 | molecular_function | cysteine-type endopeptidase activity |
C | 0008242 | molecular_function | omega peptidase activity |
C | 0016740 | molecular_function | transferase activity |
D | 0003723 | molecular_function | RNA binding |
D | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006351 | biological_process | DNA-templated transcription |
D | 0039694 | biological_process | viral RNA genome replication |
E | 0004197 | molecular_function | cysteine-type endopeptidase activity |
E | 0008242 | molecular_function | omega peptidase activity |
E | 0016740 | molecular_function | transferase activity |
F | 0004197 | molecular_function | cysteine-type endopeptidase activity |
F | 0008242 | molecular_function | omega peptidase activity |
F | 0016740 | molecular_function | transferase activity |
Functional Information from PROSITE/UniProt
site_id | PS00213 |
Number of Residues | 12 |
Details | LIPOCALIN Lipocalin signature. GTS..KFYGGWHNM |
Chain | Residue | Details |
A | GLY590-MET601 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | SITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 |
Chain | Residue | Details |
D | SER759 | |
D | ASP760 | |
D | ASP761 | |
C | GLN83 | |
F | GLN83 | |
A | ASP761 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ |
Chain | Residue | Details |
A | ASN209 | |
A | ASP218 | |
D | ASN209 | |
D | ASP218 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01344, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ |
Chain | Residue | Details |
A | CYS306 | |
D | CYS310 | |
A | CYS310 | |
D | HIS295 | |
D | CYS301 | |
D | CYS306 | |
A | HIS295 | |
A | CYS301 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01293, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ |
Chain | Residue | Details |
A | HIS642 | |
A | CYS646 | |
D | CYS487 | |
D | HIS642 | |
D | CYS646 | |
A | CYS487 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01293, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33232691 |
Chain | Residue | Details |
A | CYS645 | |
D | CYS645 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 |
Chain | Residue | Details |
A | GLN932 | |
D | GLN932 |