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1DYL

9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
D0004252molecular_functionserine-type endopeptidase activity
D0006508biological_processproteolysis
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027
ChainResidueDetails
AHIS145
AASP167
BHIS145
BASP167
CHIS145
CASP167
DHIS145
DASP167

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027, ECO:0000269|PubMed:3553612
ChainResidueDetails
ASER219
BSER219
CSER219
DSER219

site_idSWS_FT_FI3
Number of Residues8
DetailsSITE: Involved in dimerization of the capsid protein => ECO:0000250|UniProtKB:Q86925
ChainResidueDetails
ATYR193
AASN226
BTYR193
BASN226
CTYR193
CASN226
DTYR193
DASN226

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Cleavage; by autolysis => ECO:0000269|PubMed:3553612
ChainResidueDetails
ATRP267
BTRP267
CTRP267
DTRP267

223166

PDB entries from 2024-07-31

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