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7BV2

The nsp12-nsp7-nsp8 complex bound to the template-primer RNA and triphosphate form of Remdesivir(RTP)

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
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 Residues4
Detailsbinding site for residue ZN A 1002
ChainResidue
ACYS487
AHIS642
ACYS645
ACYS646

site_idAC3
Number of Residues4
Detailsbinding site for residue POP A 1003
ChainResidue
AASP623
AMG1004
PF86101
AARG553

site_idAC4
Number of Residues4
Detailsbinding site for residue MG A 1004
ChainResidue
ATYR619
AASP760
APOP1003
PF86101

site_idAC5
Number of Residues2
Detailsbinding site for residue MG A 1005
ChainResidue
AASP761
PU20

site_idAC6
Number of Residues11
Detailsbinding site for residue F86 P 101
ChainResidue
AARG555
AASP623
ASER682
ATHR687
AASN691
AASP760
APOP1003
AMG1004
PU20
TU10
TA11

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 Residues2
DetailsSITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3
ChainResidueDetails
CMET0
CGLN83
AASP761

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ
ChainResidueDetails
AASN209
AASP218

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01344, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33232691, ECO:0007744|PDB:7CYQ
ChainResidueDetails
AHIS295
ACYS301
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 Residues2
DetailsSITE: Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3
ChainResidueDetails
AMET0
AGLN932

218853

PDB entries from 2024-04-24

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