Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7EGQ

Co-transcriptional capping machineries in SARS-CoV-2 RTC: Coupling of N7-methyltransferase and 3'-5' exoribonuclease with polymerase reveals mechanisms for capping and proofreading

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
H	0003723	molecular_function	RNA binding
H	0008270	molecular_function	zinc ion binding
H	0019079	biological_process	viral genome replication
K	0000175	molecular_function	3'-5'-RNA exonuclease activity
K	0004482	molecular_function	mRNA 5'-cap (guanine-N7-)-methyltransferase activity
K	0004532	molecular_function	RNA exonuclease activity
K	0008168	molecular_function	methyltransferase activity
N	0003723	molecular_function	RNA binding
N	0003968	molecular_function	RNA-dependent RNA polymerase activity
N	0005524	molecular_function	ATP binding
N	0006351	biological_process	DNA-templated transcription
N	0039694	biological_process	viral RNA genome replication
O	0004197	molecular_function	cysteine-type endopeptidase activity
O	0008242	molecular_function	omega peptidase activity
O	0016740	molecular_function	transferase activity
P	0004197	molecular_function	cysteine-type endopeptidase activity
P	0008242	molecular_function	omega peptidase activity
P	0016740	molecular_function	transferase activity
Q	0004197	molecular_function	cysteine-type endopeptidase activity
Q	0008242	molecular_function	omega peptidase activity
Q	0016740	molecular_function	transferase activity
R	0004386	molecular_function	helicase activity
R	0005524	molecular_function	ATP binding
R	0008270	molecular_function	zinc ion binding
S	0004386	molecular_function	helicase activity
S	0005524	molecular_function	ATP binding
S	0008270	molecular_function	zinc ion binding
T	0003723	molecular_function	RNA binding
T	0019079	biological_process	viral genome replication
U	0003723	molecular_function	RNA binding
U	0008270	molecular_function	zinc ion binding
U	0019079	biological_process	viral genome replication
X	0000175	molecular_function	3'-5'-RNA exonuclease activity
X	0004482	molecular_function	mRNA 5'-cap (guanine-N7-)-methyltransferase activity
X	0004532	molecular_function	RNA exonuclease activity
X	0008168	molecular_function	methyltransferase 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	10
Details	ACT_SITE: ACT_SITE => ECO:0000255\|PROSITE-ProRule:PRU01298

Chain	Residue	Details
K	ASP90
X	ASP273
U	HIS83
U	CYS90
U	CYS117
U	CYS120
U	CYS128
U	CYS130
R	CYS26
R	CYS29
R	HIS33
K	GLU92
R	HIS39
R	CYS50
R	CYS55
R	CYS72
R	HIS75
F	CYS5
F	CYS8
F	CYS16
F	CYS19
F	CYS26
K	GLU191
F	CYS29
F	HIS33
F	HIS39
F	CYS50
F	CYS55
F	CYS72
F	HIS75
S	CYS5
S	CYS8
S	CYS16
K	HIS268
S	CYS19
S	CYS26
S	CYS29
S	HIS33
S	HIS39
S	CYS50
S	CYS55
S	CYS72
S	HIS75
K	ASP273
X	ASP90
X	GLU92
X	GLU191
X	HIS268

site_id	SWS_FT_FI2
Number of Residues	34
Details	BINDING: BINDING => ECO:0000269\|PubMed:36546776

Chain	Residue	Details
K	ASP90
K	HIS264
K	HIS268
K	ASP273
K	CYS279
K	CYS452
K	CYS477
K	CYS484
K	HIS487
X	ASP90
X	GLU92
K	GLU92
X	GLU191
X	CYS207
X	CYS210
X	CYS226
X	HIS229
X	HIS257
X	CYS261
X	HIS264
X	HIS268
X	ASP273
K	GLU191
X	CYS279
X	CYS452
X	CYS477
X	CYS484
X	HIS487
K	CYS207
K	CYS210
K	CYS226
K	HIS229
K	HIS257
K	CYS261

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01299

Chain	Residue	Details
K	ASP331
X	ASP331
F	GLN601
S	GLN601
N	HIS295
N	CYS301
N	CYS306
N	CYS310

site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Cleavage; by 3CL-PRO => ECO:0000250\|UniProtKB:P0C6V3

Chain	Residue	Details
K	GLN527
X	GLN527
A	CYS646
N	CYS487
N	HIS642
N	CYS646

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
N	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
N	GLN932

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)