8XCH
SARS-CoV-2 Replication-Transcription Complex has a dimer-of-dimeric architecture (ddRTC) in pre-capping initiation.
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 | 96 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00986, ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ |
Chain | Residue | Details |
E | CYS5 | |
E | CYS55 | |
E | CYS72 | |
E | HIS75 | |
F | CYS5 | |
F | CYS8 | |
F | CYS16 | |
F | CYS19 | |
F | CYS26 | |
F | CYS29 | |
F | HIS33 | |
E | CYS8 | |
F | HIS39 | |
F | CYS50 | |
F | CYS55 | |
F | CYS72 | |
F | HIS75 | |
M | CYS5 | |
M | CYS8 | |
M | CYS16 | |
M | CYS19 | |
M | CYS26 | |
E | CYS16 | |
M | CYS29 | |
M | HIS33 | |
M | HIS39 | |
M | CYS50 | |
M | CYS55 | |
M | CYS72 | |
M | HIS75 | |
N | CYS5 | |
N | CYS8 | |
N | CYS16 | |
E | CYS19 | |
N | CYS19 | |
N | CYS26 | |
N | CYS29 | |
N | HIS33 | |
N | HIS39 | |
N | CYS50 | |
N | CYS55 | |
N | CYS72 | |
N | HIS75 | |
U | CYS5 | |
E | CYS26 | |
U | CYS8 | |
U | CYS16 | |
U | CYS19 | |
U | CYS26 | |
U | CYS29 | |
U | HIS33 | |
U | HIS39 | |
U | CYS50 | |
U | CYS55 | |
U | CYS72 | |
E | CYS29 | |
U | HIS75 | |
V | CYS5 | |
V | CYS8 | |
V | CYS16 | |
V | CYS19 | |
V | CYS26 | |
V | CYS29 | |
V | HIS33 | |
V | HIS39 | |
V | CYS50 | |
E | HIS33 | |
V | CYS55 | |
V | CYS72 | |
V | HIS75 | |
c | CYS5 | |
c | CYS8 | |
c | CYS16 | |
c | CYS19 | |
c | CYS26 | |
c | CYS29 | |
c | HIS33 | |
E | HIS39 | |
c | HIS39 | |
c | CYS50 | |
c | CYS55 | |
c | CYS72 | |
c | HIS75 | |
d | CYS5 | |
d | CYS8 | |
d | CYS16 | |
d | CYS19 | |
d | CYS26 | |
E | CYS50 | |
d | CYS29 | |
d | HIS33 | |
d | HIS39 | |
d | CYS50 | |
d | CYS55 | |
d | CYS72 | |
d | HIS75 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00990 |
Chain | Residue | Details |
E | GLY282 | |
F | GLY282 | |
M | GLY282 | |
N | GLY282 | |
U | GLY282 | |
V | GLY282 | |
c | GLY282 | |
d | GLY282 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 |
Chain | Residue | Details |
E | GLN601 | |
Q | CYS301 | |
Q | CYS306 | |
Q | CYS310 | |
Y | HIS295 | |
Y | CYS301 | |
Y | CYS306 | |
Y | CYS310 | |
F | GLN601 | |
M | GLN601 | |
N | GLN601 | |
U | GLN601 | |
V | GLN601 | |
c | GLN601 | |
d | GLN601 | |
Q | HIS295 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
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 | |
Y | CYS487 | |
Y | HIS642 | |
Y | CYS646 | |
A | HIS642 | |
A | CYS646 | |
I | CYS487 | |
I | HIS642 | |
I | CYS646 | |
Q | CYS487 | |
Q | HIS642 | |
Q | CYS646 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
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 | |
I | CYS645 | |
Q | CYS645 | |
Y | CYS645 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | SITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 |
Chain | Residue | Details |
A | GLN932 | |
I | GLN932 | |
Q | GLN932 | |
Y | GLN932 |