Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
A0001172biological_processRNA-templated transcription
A0003968molecular_functionRNA-dependent 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
A0008168molecular_functionmethyltransferase activity
A0016740molecular_functiontransferase 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
A1990606molecular_functionmembrane scission GTPase motor activity
P0001172biological_processRNA-templated transcription
P0003968molecular_functionRNA-dependent 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 Residues1
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000269|PubMed:24257610
ChainResidueDetails
PTYR14

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by host CK2 => ECO:0000269|PubMed:8525614
ChainResidueDetails
PSER60
PSER64
ALYS1795
AGLU1833

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by host CK2 => ECO:0000269|PubMed:8525614
ChainResidueDetails
PTHR62
AASP714

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by host => ECO:0000250
ChainResidueDetails
PSER226
PSER227
ACYS1299
ACYS1302

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:26144317
ChainResidueDetails
ACYS1120
ACYS1123
AHIS1294
AHIS1296

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
ALEU1667

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon