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6U1X

Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor (3.0 A resolution)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001172biological_processRNA-templated transcription
A0003824molecular_functioncatalytic activity
A0003924molecular_functionGTPase activity
A0003968molecular_functionRNA-directed RNA polymerase activity
A0004482molecular_functionmRNA 5'-cap (guanine-N7-)-methyltransferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0006139biological_processnucleobase-containing compound metabolic process
A0006370biological_process7-methylguanosine mRNA capping
A0006397biological_processmRNA processing
A0008168molecular_functionmethyltransferase activity
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0016787molecular_functionhydrolase activity
A0019083biological_processviral transcription
A0030430cellular_componenthost cell cytoplasm
A0032259biological_processmethylation
A0034062molecular_function5'-3' RNA polymerase activity
A0039689biological_processnegative stranded viral RNA replication
A0044423cellular_componentvirion component
A0046872molecular_functionmetal ion binding
A0106005biological_processRNA 5'-cap (guanine-N7)-methylation
P0001172biological_processRNA-templated transcription
P0003968molecular_functionRNA-directed RNA polymerase activity
P0005515molecular_functionprotein binding
P0016310biological_processphosphorylation
P0019079biological_processviral genome replication
P0019083biological_processviral transcription
P0030430cellular_componenthost cell cytoplasm
P0034337biological_processRNA folding
P0044423cellular_componentvirion component
P0140691molecular_functionRNA folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 3000
ChainResidue
ACYS1081
AGLU1108
ACYS1299
ACYS1302

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 3001
ChainResidue
ACYS1120
ACYS1123
AHIS1294
AHIS1296

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Involved in oligomerization => ECO:0000250|UniProtKB:P04880
ChainResidueDetails
PTRP138
PTHR141

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000269|PubMed:24257610
ChainResidueDetails
PTYR14
AASP1762
ALYS1795
AGLU1833

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by host CK2 => ECO:0000269|PubMed:8525614
ChainResidueDetails
PSER60
PSER64

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by host CK2 => ECO:0000269|PubMed:8525614
ChainResidueDetails
PTHR62
AGLU1108
ACYS1299
ACYS1302

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by host => ECO:0000250|UniProtKB:P04880
ChainResidueDetails
PSER226
PSER227
AHIS1294
AHIS1296

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04880
ChainResidueDetails
PSER233

site_idSWS_FT_FI7
Number of Residues9
DetailsSITE: Interaction with the phosphoprotein => ECO:0000269|PubMed:31914397
ChainResidueDetails
AASN704
AARG1419
AARG1427
AGLU1496
AGLY1911
AASP1981
ALYS2022
ALEU2097
ALYS2098

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Important for escaping from the 3'-terminal leader promotter followed by the formation of a stable leaderRNA elongation complex => ECO:0000269|PubMed:35108335
ChainResidueDetails
AARG1183

237992

PDB entries from 2025-06-25

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