Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1T6B

Crystal structure of B. anthracis Protective Antigen complexed with human Anthrax toxin receptor

Functional Information from GO Data
ChainGOidnamespacecontents
X0005515molecular_functionprotein binding
X0005576cellular_componentextracellular region
X0016020cellular_componentmembrane
X0020002cellular_componenthost cell plasma membrane
X0042802molecular_functionidentical protein binding
X0043409biological_processnegative regulation of MAPK cascade
X0044164cellular_componenthost cell cytosol
X0044174cellular_componenthost cell endosome
X0044175cellular_componenthost cell endosome membrane
X0044533biological_processpositive regulation of apoptotic process in another organism
X0046872molecular_functionmetal ion binding
X0051260biological_processprotein homooligomerization
X0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA X 800
ChainResidue
XASP177
XASP179
XASP181
XILE183
XGLU188

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA X 801
ChainResidue
XLYS225
XASP235
XASP179
XASP181
XGLU188
XSER222

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN Y 303
ChainResidue
XASP683
YSER52
YSER54
YTHR118
YHOH401
YHOH402

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA X 802
ChainResidue
XHIS263
XVAL264
XSER330
XLEU450
XTHR452

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA X 803
ChainResidue
XTYR233
XILE243
XASP244
XALA460
XTHR461
XTYR462
XHOH819

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 X 804
ChainResidue
XSER294
XSER296
XLYS703
XHOH845

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15079089, ECO:0007744|PDB:1SHU, ECO:0007744|PDB:1T6B
ChainResidueDetails
YSER52
YSER54
YTHR118

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
YTHR147
XASP181
XILE183

site_idSWS_FT_FI3
Number of Residues1
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
XASP179

site_idSWS_FT_FI4
Number of Residues1
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
XGLU188

site_idSWS_FT_FI5
Number of Residues2
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
XSER222
XLYS225

site_idSWS_FT_FI6
Number of Residues1
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
XASP235

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Cleavage; by FURIN => ECO:0000269|PubMed:11207581, ECO:0000269|PubMed:1438214, ECO:0000269|PubMed:1644824
ChainResidueDetails
XARG167

site_idSWS_FT_FI8
Number of Residues4
DetailsSITE: Alpha-clamp => ECO:0000269|PubMed:21037566
ChainResidueDetails
XARG178
XLEU187
XPHE236
XPHE464

site_idSWS_FT_FI9
Number of Residues1
DetailsSITE: Cleavage; by chymotrypsin; required for translocation of LF and EF => ECO:0000269|PubMed:7961869
ChainResidueDetails
XPHE314

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Phi-clamp => ECO:0000269|PubMed:16051798, ECO:0000269|PubMed:25778700
ChainResidueDetails
XPHE427

site_idSWS_FT_FI11
Number of Residues1
DetailsSITE: Essential for binding to cell receptor => ECO:0000269|PubMed:12771151
ChainResidueDetails
XASP683

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon