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3J0C

Models of E1, E2 and CP of Venezuelan Equine Encephalitis Virus TC-83 strain restrained by a near atomic resolution cryo-EM map

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0019028cellular_componentviral capsid
A0055036cellular_componentvirion membrane
B0005198molecular_functionstructural molecule activity
B0019028cellular_componentviral capsid
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
D0004252molecular_functionserine-type endopeptidase activity
D0019028cellular_componentviral capsid
D0055036cellular_componentvirion membrane
E0005198molecular_functionstructural molecule activity
E0019028cellular_componentviral capsid
F0004252molecular_functionserine-type endopeptidase activity
F0006508biological_processproteolysis
G0004252molecular_functionserine-type endopeptidase activity
G0019028cellular_componentviral capsid
G0055036cellular_componentvirion membrane
H0005198molecular_functionstructural molecule activity
H0019028cellular_componentviral capsid
I0004252molecular_functionserine-type endopeptidase activity
I0006508biological_processproteolysis
J0004252molecular_functionserine-type endopeptidase activity
J0019028cellular_componentviral capsid
J0055036cellular_componentvirion membrane
K0005198molecular_functionstructural molecule activity
K0019028cellular_componentviral capsid
L0004252molecular_functionserine-type endopeptidase activity
L0006508biological_processproteolysis
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027
ChainResidueDetails
CHIS152
LHIS152
LASP174
LSER226
CASP174
CSER226
FHIS152
FASP174
FSER226
IHIS152
IASP174
ISER226

site_idSWS_FT_FI2
Number of Residues8
DetailsSITE: Involved in dimerization of the capsid protein => ECO:0000250|UniProtKB:Q86925
ChainResidueDetails
CTYR200
CASN233
FTYR200
FASN233
ITYR200
IASN233
LTYR200
LASN233

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P03315
ChainResidueDetails
CTRP275
FTRP275
ITRP275
LTRP275

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09592
ChainResidueDetails
CSER124
KCYS396
KCYS416
KCYS417
FSER124
ISER124
LSER124
ECYS416
ECYS417
HCYS396
HCYS416
HCYS417

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P09592
ChainResidueDetails
CTHR127
FTHR127
ITHR127
LTHR127
HASN212
HASN318
KASN212
KASN318

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PDB entries from 2024-05-01

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