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6XOB

CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP with Fab EEEV-143.

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 PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
NTYR191-HIS197

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027
ChainResidueDetails
CHIS138
LHIS138
LASP160
LSER212
CASP160
CSER212
FHIS138
FASP160
FSER212
IHIS138
IASP160
ISER212

site_idSWS_FT_FI2
Number of Residues8
DetailsSITE: Involved in dimerization of the capsid protein => ECO:0000250|UniProtKB:Q86925
ChainResidueDetails
CTYR186
CASN219
FTYR186
FASN219
ITYR186
IASN219
LTYR186
LASN219

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P03315
ChainResidueDetails
CTRP261
FTRP261
ITRP261
LTRP261

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09592
ChainResidueDetails
CSER110
FSER110
ISER110
LSER110

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P09592
ChainResidueDetails
CTHR113
KCYS393
KCYS413
KCYS414
FTHR113
ITHR113
LTHR113
ECYS413
ECYS414
HCYS393
HCYS413
HCYS414

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PDB entries from 2024-07-17

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