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4FTS

Crystal structure of the N363T mutant of the Flock House virus capsid

Replaces:  2Q23
Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0039617cellular_componentT=3 icosahedral viral capsid
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
B0039617cellular_componentT=3 icosahedral viral capsid
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
C0039617cellular_componentT=3 icosahedral viral capsid
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
AHOH659
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 EPE A 503
ChainResidue
AGLY258
AGLN260
ATHR261
APRO264
AALA265
AALA282
AGLU283
CGLN201
CPHE202
CPRO203

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 501
ChainResidue
BASP221
BGLY273
BHOH678
CTHR157
CSER160
CASP161
CGLU257

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 502
ChainResidue
BSER102

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EPE B 503
ChainResidue
AGLN201
APRO203
BGLY258
BGLN260
BTHR261
BPRO264
BALA265
BGLU283

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA C 501
ChainResidue
AASP161
CASP221
CGLY273

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C 502
ChainResidue
ASER211
ALEU213
BSER211
BSER212
BLEU213
CSER211
CSER212
CLEU213

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EPE C 503
ChainResidue
BGLN201
BPHE202
BPRO203
CSER156
CGLY258
CGLN260
CTHR261
CPRO264
CALA265

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:19553341
ChainResidueDetails
AASP75
BASP75
CASP75

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0007744|PDB:4FTS
ChainResidueDetails
AASP161
BASP161
CASP161

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0007744|PDB:4FTB
ChainResidueDetails
AASP221
AGLY273
BASP221
BGLY273
CASP221
CGLY273

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0007744|PDB:4FSJ
ChainResidueDetails
AASP249
AGLU251
BASP249
BGLU251
CASP249
CGLU251

site_idSWS_FT_FI5
Number of Residues3
DetailsSITE: Cleavage; by autolysis => ECO:0000269|PubMed:1404613
ChainResidueDetails
ATHR363
BTHR363
CTHR363

site_idSWS_FT_FI6
Number of Residues9
DetailsSITE: Interaction with viral RNA genome => ECO:0000269|PubMed:9765417
ChainResidueDetails
APHE402
APHE405
APHE407
BPHE402
BPHE405
BPHE407
CPHE402
CPHE405
CPHE407

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PDB entries from 2024-07-17

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