7N0D

Cryo-EM structure of the tetrameric form of SARS-CoV-2 nsp10-nsp14 (E191A)-RNA complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0008270	molecular_function	zinc ion binding
A	0019079	biological_process	viral genome replication
B	0000175	molecular_function	3'-5'-RNA exonuclease activity
B	0004482	molecular_function	mRNA 5'-cap (guanine-N7-)-methyltransferase activity
B	0004532	molecular_function	RNA exonuclease activity
B	0008168	molecular_function	methyltransferase activity
C	0003723	molecular_function	RNA binding
C	0008270	molecular_function	zinc ion binding
C	0019079	biological_process	viral genome replication
D	0000175	molecular_function	3'-5'-RNA exonuclease activity
D	0004482	molecular_function	mRNA 5'-cap (guanine-N7-)-methyltransferase activity
D	0004532	molecular_function	RNA exonuclease activity
D	0008168	molecular_function	methyltransferase activity
E	0003723	molecular_function	RNA binding
E	0008270	molecular_function	zinc ion binding
E	0019079	biological_process	viral genome replication
F	0000175	molecular_function	3'-5'-RNA exonuclease activity
F	0004482	molecular_function	mRNA 5'-cap (guanine-N7-)-methyltransferase activity
F	0004532	molecular_function	RNA exonuclease activity
F	0008168	molecular_function	methyltransferase activity
G	0003723	molecular_function	RNA binding
G	0008270	molecular_function	zinc ion binding
G	0019079	biological_process	viral genome replication
H	0000175	molecular_function	3'-5'-RNA exonuclease activity
H	0004482	molecular_function	mRNA 5'-cap (guanine-N7-)-methyltransferase activity
H	0004532	molecular_function	RNA exonuclease activity
H	0008168	molecular_function	methyltransferase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01298

Chain	Residue	Details
B	ASP90
D	ASP273
F	ASP90
F	GLU92
F	ALA191
F	HIS268
F	ASP273
H	ASP90
H	GLU92
H	ALA191
H	HIS268
B	GLU92
H	ASP273
E	CYS117
E	CYS120
E	CYS128
E	CYS130
G	CYS74
G	CYS77
G	HIS83
G	CYS90
G	CYS117
B	ALA191
G	CYS120
G	CYS128
G	CYS130
B	HIS268
B	ASP273
D	ASP90
D	GLU92
D	ALA191
D	HIS268

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site_id	SWS_FT_FI2
Number of Residues	68
Details	BINDING: BINDING => ECO:0000269|PubMed:36546776

Chain	Residue	Details
B	ASP90
B	HIS264
B	HIS268
B	ASP273
B	CYS279
B	CYS452
B	CYS477
B	CYS484
B	HIS487
D	ASP90
D	GLU92
B	GLU92
D	ALA191
D	CYS207
D	CYS210
D	CYS226
D	HIS229
D	HIS257
D	CYS261
D	HIS264
D	HIS268
D	ASP273
B	ALA191
D	CYS279
D	CYS452
D	CYS477
D	CYS484
D	HIS487
F	ASP90
F	GLU92
F	ALA191
F	CYS207
F	CYS210
B	CYS207
F	CYS226
F	HIS229
F	HIS257
F	CYS261
F	HIS264
F	HIS268
F	ASP273
F	CYS279
F	CYS452
F	CYS477
B	CYS210
F	CYS484
F	HIS487
H	ASP90
H	GLU92
H	ALA191
H	CYS207
H	CYS210
H	CYS226
H	HIS229
H	HIS257
B	CYS226
H	CYS261
H	HIS264
H	HIS268
H	ASP273
H	CYS279
H	CYS452
H	CYS477
H	CYS484
H	HIS487
B	HIS229
B	HIS257
B	CYS261

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01299

Chain	Residue	Details
B	ASP331
D	ASP331
F	ASP331
H	ASP331

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site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3

Chain	Residue	Details
B	GLN527
D	GLN527
F	GLN527
H	GLN527

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