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6XEZ

Structure of SARS-CoV-2 replication-transcription complex bound to nsp13 helicase - nsp13(2)-RTC

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0003968molecular_functionRNA-dependent 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
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1001
ChainResidue
AHIS295
ACYS301
ACYS306
ACYS310

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 1002
ChainResidue
ACYS487
APHE571
AHIS642
ACYS645
ACYS646

site_idAC3
Number of Residues3
Detailsbinding site for residue MG A 1003
ChainResidue
AASN209
AASP218
AADP1004

site_idAC4
Number of Residues9
Detailsbinding site for residue ADP A 1004
ChainResidue
AASN52
ALYS73
AHIS75
AASN79
AARG116
AASN209
ATYR217
AASP218
AMG1003

site_idAC5
Number of Residues2
Detailsbinding site for residue 1N7 A 1005
ChainResidue
AVAL204
AILE223

site_idAC6
Number of Residues2
Detailsbinding site for residue 1N7 A 1006
ChainResidue
AARG197
ALYS288

site_idAC7
Number of Residues5
Detailsbinding site for residue ZN E 701
ChainResidue
ECYS5
ECYS8
ECYS26
ECYS29
EGLY99

site_idAC8
Number of Residues5
Detailsbinding site for residue ZN E 702
ChainResidue
ECYS50
EALA52
ECYS55
ECYS72
EHIS75

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN E 703
ChainResidue
ECYS16
ECYS19
EHIS33
EHIS39

site_idAD1
Number of Residues9
Detailsbinding site for residue ADP E 704
ChainResidue
EPRO283
EGLY285
ETHR286
EGLY287
ELYS288
EHIS290
EARG443
EGLU540
EAF3705

site_idAD2
Number of Residues6
Detailsbinding site for residue AF3 E 705
ChainResidue
EGLY285
ETHR286
ELYS288
EGLU375
EADP704
EMG706

site_idAD3
Number of Residues2
Detailsbinding site for residue MG E 706
ChainResidue
ESER289
EAF3705

site_idAD4
Number of Residues4
Detailsbinding site for residue 1N7 E 707
ChainResidue
AVAL905
EVAL45
ETYR70
EPHE90

site_idAD5
Number of Residues5
Detailsbinding site for residue ZN F 1000
ChainResidue
FCYS5
FCYS8
FCYS26
FCYS29
FGLY99

site_idAD6
Number of Residues5
Detailsbinding site for residue ZN F 1001
ChainResidue
FCYS50
FALA52
FCYS55
FCYS72
FHIS75

site_idAD7
Number of Residues4
Detailsbinding site for residue ZN F 1002
ChainResidue
FCYS16
FCYS19
FHIS33
FHIS39

site_idAD8
Number of Residues10
Detailsbinding site for residue ADP F 1003
ChainResidue
FGLY282
FPRO283
FPRO284
FGLY285
FTHR286
FGLY287
FLYS288
FLYS320
FARG442
FAF31004

site_idAD9
Number of Residues7
Detailsbinding site for residue AF3 F 1004
ChainResidue
FGLY282
FPRO284
FTHR286
FLYS288
FASP374
FADP1003
FMG1005

site_idAE1
Number of Residues4
Detailsbinding site for residue MG F 1005
ChainResidue
FLYS288
FSER289
FASP374
FAF31004

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
FGLY282

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 Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01293, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ
ChainResidueDetails
ACYS487
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

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3
ChainResidueDetails
AGLN932

222624

PDB entries from 2024-07-17

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