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4FTE

Crystal structure of the D75N mutant capsid of Flock House virus

Replaces:  2Q25
Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0019028cellular_componentviral capsid
A0039617cellular_componentT=3 icosahedral viral capsid
A0044423cellular_componentvirion component
A0046718biological_processsymbiont entry into host cell
A0046872molecular_functionmetal ion binding
A0140267biological_processsymbiont entry into host cell via permeabilization of host membrane
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0019028cellular_componentviral capsid
B0039617cellular_componentT=3 icosahedral viral capsid
B0044423cellular_componentvirion component
B0046718biological_processsymbiont entry into host cell
B0046872molecular_functionmetal ion binding
B0140267biological_processsymbiont entry into host cell via permeabilization of host membrane
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0016787molecular_functionhydrolase activity
C0019028cellular_componentviral capsid
C0039617cellular_componentT=3 icosahedral viral capsid
C0044423cellular_componentvirion component
C0046718biological_processsymbiont entry into host cell
C0046872molecular_functionmetal ion binding
C0140267biological_processsymbiont entry into host cell via permeabilization of host membrane
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 501
ChainResidue
AASP221
AGLY273
AHOH645
BASP161

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 502
ChainResidue
AASP249
AGLU251
BASP249
CASP249
CGLU251

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
ASER211
ASER212
ALEU213
AHOH673
BSER211
BSER212
BLEU213
CSER211
CSER212
CLEU213

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EPE A 504
ChainResidue
AGLY258
AGLN260
ATHR261
APRO264
AALA265
AALA282
AGLU283
CGLN201
CPHE202
CPRO203

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 501
ChainResidue
BASP221
BGLY273
CSER160
CASP161
CGLU257

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 502
ChainResidue
BSER102

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EPE B 503
ChainResidue
AGLN201
APRO203
BGLY258
BGLN260
BTHR261
BPRO264
BALA265
BGLU283

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 501
ChainResidue
AASP161
CASP221
CGLY273
CHOH646

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EPE C 502
ChainResidue
BGLN201
BPHE202
BPRO203
CGLY258
CGLN260
CTHR261
CPRO264
CALA265
CGLU283

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"evidences":[{"source":"PubMed","id":"19553341","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PDB","id":"4FTS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PDB","id":"4FTB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PDB","id":"4FSJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsSite: {"description":"Cleavage; by autolysis","evidences":[{"source":"PubMed","id":"1404613","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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