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3KWV

Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0051260biological_processprotein homooligomerization
B0005576cellular_componentextracellular region
B0051260biological_processprotein homooligomerization
C0003824molecular_functioncatalytic activity
C0005576cellular_componentextracellular region
C0008237molecular_functionmetallopeptidase activity
C0046872molecular_functionmetal ion binding
D0005576cellular_componentextracellular region
D0051260biological_processprotein homooligomerization
E0005576cellular_componentextracellular region
E0051260biological_processprotein homooligomerization
F0003824molecular_functioncatalytic activity
F0005576cellular_componentextracellular region
F0008237molecular_functionmetallopeptidase activity
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 736
ChainResidue
AASP177
AASP179
AASP181
AILE183
AGLU188
AHOH738

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 737
ChainResidue
ASER222
ALYS225
AASP235
AASP179
AASP181
AGLU188

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 736
ChainResidue
BASP177
BASP179
BASP181
BILE183
BGLU188
BHOH738

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 737
ChainResidue
BASP179
BASP181
BGLU188
BSER222
BLYS225
BASP235

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 736
ChainResidue
DASP177
DASP179
DASP181
DILE183
DGLU188
DHOH738

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 737
ChainResidue
DASP179
DASP181
DGLU188
DSER222
DLYS225
DASP235

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 736
ChainResidue
EASP177
EASP179
EASP181
EILE183
EGLU188
EHOH738

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 737
ChainResidue
EASP179
EASP181
EGLU188
ESER222
ELYS225
EASP235

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsTRANSMEM: Beta stranded => ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164, ECO:0007744|PDB:3J9C, ECO:0007744|PDB:6PSN, ECO:0007744|PDB:6UZB, ECO:0007744|PDB:6UZD, ECO:0007744|PDB:6UZE
ChainResidueDetails
AGLU302-ALA333
AHIS336-THR345
BGLU302-ALA333
BHIS336-THR345
DGLU302-ALA333
DHIS336-THR345
EGLU302-ALA333
EHIS336-THR345

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:15243628, ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566, ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164, ECO:0000269|PubMed:9039918, ECO:0007744|PDB:1ACC, ECO:0007744|PDB:1T6B, ECO:0007744|PDB:1TZN, ECO:0007744|PDB:1TZO, ECO:0007744|PDB:3J9C, ECO:0007744|PDB:3KWV, ECO:0007744|PDB:6PSN, ECO:0007744|PDB:6UZB, ECO:0007744|PDB:6UZD, ECO:0007744|PDB:6UZE
ChainResidueDetails
AASP177
EASP177
EASP181
EILE183
AASP181
AILE183
BASP177
BASP181
BILE183
DASP177
DASP181
DILE183

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15243628, ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566, ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164, ECO:0000269|PubMed:9039918, ECO:0007744|PDB:1ACC, ECO:0007744|PDB:1T6B, ECO:0007744|PDB:1TZO, ECO:0007744|PDB:3J9C, ECO:0007744|PDB:3KWV, ECO:0007744|PDB:6PSN, ECO:0007744|PDB:6UZB, ECO:0007744|PDB:6UZD, ECO:0007744|PDB:6UZE
ChainResidueDetails
AASP179
BASP179
DASP179
EASP179

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566, ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164, ECO:0007744|PDB:1ACC, ECO:0007744|PDB:1TZN, ECO:0007744|PDB:1TZO, ECO:0007744|PDB:3J9C, ECO:0007744|PDB:3KWV, ECO:0007744|PDB:6PSN, ECO:0007744|PDB:6UZB, ECO:0007744|PDB:6UZD, ECO:0007744|PDB:6UZE
ChainResidueDetails
AGLU188
BGLU188
DGLU188
EGLU188

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15243628, ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566, ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164, ECO:0007744|PDB:1ACC, ECO:0007744|PDB:1T6B, ECO:0007744|PDB:1TZN, ECO:0007744|PDB:1TZO, ECO:0007744|PDB:3J9C, ECO:0007744|PDB:3KWV, ECO:0007744|PDB:6PSN, ECO:0007744|PDB:6UZB, ECO:0007744|PDB:6UZD, ECO:0007744|PDB:6UZE
ChainResidueDetails
ASER222
ALYS225
BSER222
BLYS225
DSER222
DLYS225
ESER222
ELYS225

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15243628, ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566, ECO:0000269|PubMed:32047164, ECO:0007744|PDB:1ACC, ECO:0007744|PDB:1T6B, ECO:0007744|PDB:1TZN, ECO:0007744|PDB:1TZO, ECO:0007744|PDB:3KWV, ECO:0007744|PDB:6PSN, ECO:0007744|PDB:6UZB, ECO:0007744|PDB:6UZD, ECO:0007744|PDB:6UZE
ChainResidueDetails
AASP235
BASP235
DASP235
EASP235

site_idSWS_FT_FI7
Number of Residues16
DetailsSITE: Alpha-clamp => ECO:0000269|PubMed:21037566
ChainResidueDetails
AARG178
DLEU187
DPHE236
DILE484
EARG178
ELEU187
EPHE236
EILE484
ALEU187
APHE236
AILE484
BARG178
BLEU187
BPHE236
BILE484
DARG178

site_idSWS_FT_FI8
Number of Residues4
DetailsSITE: Cleavage; by chymotrypsin; required for translocation of LF and EF => ECO:0000269|PubMed:7961869
ChainResidueDetails
AILE334
BILE334
DILE334
EILE334

site_idSWS_FT_FI9
Number of Residues4
DetailsSITE: Phi-clamp => ECO:0000269|PubMed:16051798, ECO:0000269|PubMed:25778700
ChainResidueDetails
AGLN447
BGLN447
DGLN447
EGLN447

site_idSWS_FT_FI10
Number of Residues4
DetailsSITE: Essential for binding to cell receptor => ECO:0000269|PubMed:12771151
ChainResidueDetails
ALYS703
BLYS703
DLYS703
ELYS703

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 641
ChainResidueDetails

site_idMCSA2
Number of Residues
DetailsM-CSA 641
ChainResidueDetails

222926

PDB entries from 2024-07-24

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