1T6B
Crystal structure of B. anthracis Protective Antigen complexed with human Anthrax toxin receptor
Functional Information from GO Data
Chain | GOid | namespace | contents |
X | 0005515 | molecular_function | protein binding |
X | 0005576 | cellular_component | extracellular region |
X | 0016020 | cellular_component | membrane |
X | 0020002 | cellular_component | host cell plasma membrane |
X | 0042802 | molecular_function | identical protein binding |
X | 0043409 | biological_process | negative regulation of MAPK cascade |
X | 0044164 | cellular_component | host cell cytosol |
X | 0044174 | cellular_component | host cell endosome |
X | 0044175 | cellular_component | host cell endosome membrane |
X | 0044533 | biological_process | positive regulation of apoptotic process in another organism |
X | 0046872 | molecular_function | metal ion binding |
X | 0051260 | biological_process | protein homooligomerization |
X | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA X 800 |
Chain | Residue |
X | ASP177 |
X | ASP179 |
X | ASP181 |
X | ILE183 |
X | GLU188 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA X 801 |
Chain | Residue |
X | LYS225 |
X | ASP235 |
X | ASP179 |
X | ASP181 |
X | GLU188 |
X | SER222 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN Y 303 |
Chain | Residue |
X | ASP683 |
Y | SER52 |
Y | SER54 |
Y | THR118 |
Y | HOH401 |
Y | HOH402 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA X 802 |
Chain | Residue |
X | HIS263 |
X | VAL264 |
X | SER330 |
X | LEU450 |
X | THR452 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NA X 803 |
Chain | Residue |
X | TYR233 |
X | ILE243 |
X | ASP244 |
X | ALA460 |
X | THR461 |
X | TYR462 |
X | HOH819 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 X 804 |
Chain | Residue |
X | SER294 |
X | SER296 |
X | LYS703 |
X | HOH845 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15079089, ECO:0007744|PDB:1SHU, ECO:0007744|PDB:1T6B |
Chain | Residue | Details |
Y | SER52 | |
Y | SER54 | |
Y | THR118 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
Y | THR147 | |
X | ASP181 | |
X | ILE183 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: 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 |
Chain | Residue | Details |
X | ASP179 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: 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 |
Chain | Residue | Details |
X | GLU188 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: 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 |
Chain | Residue | Details |
X | SER222 | |
X | LYS225 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: 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 |
Chain | Residue | Details |
X | ASP235 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | SITE: Cleavage; by FURIN => ECO:0000269|PubMed:11207581, ECO:0000269|PubMed:1438214, ECO:0000269|PubMed:1644824 |
Chain | Residue | Details |
X | ARG167 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | SITE: Alpha-clamp => ECO:0000269|PubMed:21037566 |
Chain | Residue | Details |
X | ARG178 | |
X | LEU187 | |
X | PHE236 | |
X | PHE464 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | SITE: Cleavage; by chymotrypsin; required for translocation of LF and EF => ECO:0000269|PubMed:7961869 |
Chain | Residue | Details |
X | PHE314 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | SITE: Phi-clamp => ECO:0000269|PubMed:16051798, ECO:0000269|PubMed:25778700 |
Chain | Residue | Details |
X | PHE427 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | SITE: Essential for binding to cell receptor => ECO:0000269|PubMed:12771151 |
Chain | Residue | Details |
X | ASP683 |