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7EIZ

Coupling of N7-methyltransferase and 3'-5' exoribonuclease with SARS-CoV-2 polymerase reveals mechanisms for capping and proofreading

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0003968molecular_functionRNA-directed RNA polymerase activity
A0005524molecular_functionATP binding
A0006351biological_processDNA-templated transcription
A0039694biological_processviral RNA genome replication
B0004197molecular_functioncysteine-type endopeptidase activity
B0008242molecular_functionomega peptidase activity
B0016740molecular_functiontransferase activity
C0004197molecular_functioncysteine-type endopeptidase activity
C0008242molecular_functionomega peptidase activity
C0016740molecular_functiontransferase activity
D0004197molecular_functioncysteine-type endopeptidase activity
D0008242molecular_functionomega peptidase activity
D0016740molecular_functiontransferase activity
E0004386molecular_functionhelicase activity
E0005524molecular_functionATP binding
E0008270molecular_functionzinc ion binding
F0004386molecular_functionhelicase activity
F0005524molecular_functionATP binding
F0008270molecular_functionzinc ion binding
G0003723molecular_functionRNA binding
G0019079biological_processviral genome replication
H0003723molecular_functionRNA binding
H0008270molecular_functionzinc ion binding
H0019079biological_processviral genome replication
K0000175molecular_function3'-5'-RNA exonuclease activity
K0004482molecular_functionmRNA 5'-cap (guanine-N7-)-methyltransferase activity
K0004532molecular_functionRNA exonuclease activity
K0008168molecular_functionmethyltransferase activity
Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues12
DetailsLIPOCALIN Lipocalin signature. GTS..KFYGGWHNM
ChainResidueDetails
AGLY590-MET601

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00986, ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ
ChainResidueDetails
ECYS5
ECYS55
ECYS72
EHIS75
FCYS5
FCYS8
FCYS16
FCYS19
FCYS26
FCYS29
FHIS33
ECYS8
FHIS39
FCYS50
FCYS55
FCYS72
FHIS75
ECYS16
ECYS19
ECYS26
ECYS29
EHIS33
EHIS39
ECYS50

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00990
ChainResidueDetails
EGLY282
KHIS264
KHIS268
KASP273
KCYS279
KCYS452
KCYS477
KCYS484
KHIS487
FGLY282
KGLU191
KCYS207
KCYS210
KCYS226
KHIS229
KHIS257
KCYS261

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3
ChainResidueDetails
EGLN601
FGLN601
ACYS306
ACYS310

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3
ChainResidueDetails
KGLN527
AHIS642
ACYS646

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01293, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33232691
ChainResidueDetails
ACYS645

237423

PDB entries from 2025-06-11

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