8GWF
A mechanism for SARS-CoV-2 RNA capping and its inhibition by nucleotide analogue inhibitors
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 | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| D | 0008242 | molecular_function | omega peptidase activity |
| D | 0016740 | molecular_function | transferase activity |
| E | 0004386 | molecular_function | helicase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0008270 | molecular_function | zinc ion binding |
| F | 0004386 | molecular_function | helicase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0008270 | molecular_function | zinc ion binding |
| G | 0003723 | molecular_function | RNA binding |
| G | 0019079 | biological_process | viral genome replication |
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 | 1 |
| Details | SITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 |
| Chain | Residue | Details |
| G | GLN113 | |
| F | CYS55 | |
| F | CYS72 | |
| F | HIS75 | |
| E | CYS5 | |
| E | CYS8 | |
| E | CYS16 | |
| E | CYS19 | |
| E | CYS26 | |
| E | CYS29 | |
| E | HIS33 | |
| F | CYS8 | |
| E | HIS39 | |
| E | CYS50 | |
| E | CYS55 | |
| E | CYS72 | |
| E | HIS75 | |
| F | CYS16 | |
| F | CYS19 | |
| F | CYS26 | |
| F | CYS29 | |
| F | HIS33 | |
| F | HIS39 | |
| F | CYS50 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00990 |
| Chain | Residue | Details |
| F | GLY282 | |
| E | GLY282 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 |
| Chain | Residue | Details |
| F | GLN601 | |
| E | GLN601 | |
| A | CYS306 | |
| A | CYS310 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| 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 | CYS487 | |
| A | HIS642 | |
| A | CYS646 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| 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 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 |
| Chain | Residue | Details |
| A | GLN932 |
