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7FFE

Cryo-EM structure of VEEV VLP

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004252molecular_functionserine-type endopeptidase activity
B0019028cellular_componentviral capsid
B0055036cellular_componentvirion membrane
C0004252molecular_functionserine-type endopeptidase activity
C0019028cellular_componentviral capsid
C0055036cellular_componentvirion membrane
F0004252molecular_functionserine-type endopeptidase activity
F0006508biological_processproteolysis
G0004252molecular_functionserine-type endopeptidase activity
G0019028cellular_componentviral capsid
G0055036cellular_componentvirion membrane
I0004252molecular_functionserine-type endopeptidase activity
I0019028cellular_componentviral capsid
I0055036cellular_componentvirion membrane
J0005198molecular_functionstructural molecule activity
J0019028cellular_componentviral capsid
K0004252molecular_functionserine-type endopeptidase activity
K0006508biological_processproteolysis
L0004252molecular_functionserine-type endopeptidase activity
L0019028cellular_componentviral capsid
L0055036cellular_componentvirion membrane
N0005198molecular_functionstructural molecule activity
N0019028cellular_componentviral capsid
O0004252molecular_functionserine-type endopeptidase activity
O0019028cellular_componentviral capsid
O0055036cellular_componentvirion membrane
P0004252molecular_functionserine-type endopeptidase activity
P0019028cellular_componentviral capsid
P0055036cellular_componentvirion membrane
Q0005198molecular_functionstructural molecule activity
Q0019028cellular_componentviral capsid
R0005198molecular_functionstructural molecule activity
R0019028cellular_componentviral capsid
S0004252molecular_functionserine-type endopeptidase activity
S0006508biological_processproteolysis
T0004252molecular_functionserine-type endopeptidase activity
T0019028cellular_componentviral capsid
T0055036cellular_componentvirion membrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
KHIS152
KASP174
KSER226
SHIS152
SASP174
SSER226
JILE368-LEU388
NILE368-LEU388
QILE368-LEU388
RILE368-LEU388
FASP174
FSER226

site_idSWS_FT_FI2
Number of Residues136
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
KTYR200
KASN233
STYR200
SASN233
JPHE389-ALA423
NPHE389-ALA423
QPHE389-ALA423
RPHE389-ALA423

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Cleavage; by host signal peptidase => ECO:0000250
ChainResidueDetails
QALA423
RALA423
JALA423
NALA423

site_idSWS_FT_FI4
Number of Residues12
DetailsLIPID: S-palmitoyl cysteine; by host => ECO:0000250
ChainResidueDetails
QCYS396
QCYS416
QCYS417
RCYS396
RCYS416
RCYS417
JCYS396
JCYS416
JCYS417
NCYS396
NCYS416
NCYS417

site_idSWS_FT_FI5
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255
ChainResidueDetails
NASN212
NASN318
QASN212
QASN318
RASN212
RASN318
JASN212
JASN318

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PDB entries from 2024-05-15

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