6ZXK
Fully-loaded anthrax lethal toxin in its heptameric pre-pore state and PA7LF(2+1B) arrangement
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0051260 | biological_process | protein homooligomerization |
B | 0005576 | cellular_component | extracellular region |
B | 0051260 | biological_process | protein homooligomerization |
C | 0005576 | cellular_component | extracellular region |
C | 0051260 | biological_process | protein homooligomerization |
D | 0005576 | cellular_component | extracellular region |
D | 0051260 | biological_process | protein homooligomerization |
E | 0005576 | cellular_component | extracellular region |
E | 0051260 | biological_process | protein homooligomerization |
F | 0005576 | cellular_component | extracellular region |
F | 0051260 | biological_process | protein homooligomerization |
G | 0005576 | cellular_component | extracellular region |
G | 0051260 | biological_process | protein homooligomerization |
H | 0003824 | molecular_function | catalytic activity |
H | 0005576 | cellular_component | extracellular region |
H | 0008237 | molecular_function | metallopeptidase activity |
H | 0046872 | molecular_function | metal ion binding |
I | 0003824 | molecular_function | catalytic activity |
I | 0005576 | cellular_component | extracellular region |
I | 0008237 | molecular_function | metallopeptidase activity |
I | 0046872 | molecular_function | metal ion binding |
J | 0003824 | molecular_function | catalytic activity |
J | 0005576 | cellular_component | extracellular region |
J | 0008237 | molecular_function | metallopeptidase activity |
J | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. GFIHEFGHAV |
Chain | Residue | Details |
H | GLY683-VAL692 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 140 |
Details | TRANSMEM: 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 |
Chain | Residue | Details |
A | GLU302-PHE313 | |
E | ILE316-SER325 | |
F | GLU302-PHE313 | |
F | ILE316-SER325 | |
G | GLU302-PHE313 | |
G | ILE316-SER325 | |
A | ILE316-SER325 | |
B | GLU302-PHE313 | |
B | ILE316-SER325 | |
C | GLU302-PHE313 | |
C | ILE316-SER325 | |
D | GLU302-PHE313 | |
D | ILE316-SER325 | |
E | GLU302-PHE313 |
site_id | SWS_FT_FI2 |
Number of Residues | 21 |
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: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 |
A | ASP177 | |
D | ASP177 | |
D | ASP181 | |
D | ILE183 | |
E | ASP177 | |
E | ASP181 | |
E | ILE183 | |
F | ASP177 | |
F | ASP181 | |
F | ILE183 | |
G | ASP177 | |
A | ASP181 | |
G | ASP181 | |
G | ILE183 | |
A | ILE183 | |
B | ASP177 | |
B | ASP181 | |
B | ILE183 | |
C | ASP177 | |
C | ASP181 | |
C | ILE183 |
site_id | SWS_FT_FI3 |
Number of Residues | 7 |
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 |
A | ASP179 | |
B | ASP179 | |
C | ASP179 | |
D | ASP179 | |
E | ASP179 | |
F | ASP179 | |
G | ASP179 |
site_id | SWS_FT_FI4 |
Number of Residues | 7 |
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 |
A | GLU188 | |
B | GLU188 | |
C | GLU188 | |
D | GLU188 | |
E | GLU188 | |
F | GLU188 | |
G | GLU188 |
site_id | SWS_FT_FI5 |
Number of Residues | 14 |
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 |
A | SER222 | |
E | LYS225 | |
F | SER222 | |
F | LYS225 | |
G | SER222 | |
G | LYS225 | |
A | LYS225 | |
B | SER222 | |
B | LYS225 | |
C | SER222 | |
C | LYS225 | |
D | SER222 | |
D | LYS225 | |
E | SER222 |
site_id | SWS_FT_FI6 |
Number of Residues | 7 |
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 |
A | ASP235 | |
B | ASP235 | |
C | ASP235 | |
D | ASP235 | |
E | ASP235 | |
F | ASP235 | |
G | ASP235 |
site_id | SWS_FT_FI7 |
Number of Residues | 7 |
Details | SITE: Cleavage; by FURIN => ECO:0000269|PubMed:11207581, ECO:0000269|PubMed:1438214, ECO:0000269|PubMed:1644824 |
Chain | Residue | Details |
A | ARG167 | |
B | ARG167 | |
C | ARG167 | |
D | ARG167 | |
E | ARG167 | |
F | ARG167 | |
G | ARG167 |
site_id | SWS_FT_FI8 |
Number of Residues | 28 |
Details | SITE: Alpha-clamp => ECO:0000269|PubMed:21037566 |
Chain | Residue | Details |
A | ARG178 | |
C | LEU187 | |
C | PHE236 | |
C | PHE464 | |
D | ARG178 | |
D | LEU187 | |
D | PHE236 | |
D | PHE464 | |
E | ARG178 | |
E | LEU187 | |
E | PHE236 | |
A | LEU187 | |
E | PHE464 | |
F | ARG178 | |
F | LEU187 | |
F | PHE236 | |
F | PHE464 | |
G | ARG178 | |
G | LEU187 | |
G | PHE236 | |
G | PHE464 | |
A | PHE236 | |
A | PHE464 | |
B | ARG178 | |
B | LEU187 | |
B | PHE236 | |
B | PHE464 | |
C | ARG178 |
site_id | SWS_FT_FI9 |
Number of Residues | 7 |
Details | SITE: Cleavage; by chymotrypsin; required for translocation of LF and EF => ECO:0000269|PubMed:7961869 |
Chain | Residue | Details |
A | PHE314 | |
B | PHE314 | |
C | PHE314 | |
D | PHE314 | |
E | PHE314 | |
F | PHE314 | |
G | PHE314 |
site_id | SWS_FT_FI10 |
Number of Residues | 7 |
Details | SITE: Phi-clamp => ECO:0000269|PubMed:16051798, ECO:0000269|PubMed:25778700 |
Chain | Residue | Details |
A | PHE427 | |
B | PHE427 | |
C | PHE427 | |
D | PHE427 | |
E | PHE427 | |
F | PHE427 | |
G | PHE427 |
site_id | SWS_FT_FI11 |
Number of Residues | 7 |
Details | SITE: Essential for binding to cell receptor => ECO:0000269|PubMed:12771151 |
Chain | Residue | Details |
A | ASP683 | |
B | ASP683 | |
C | ASP683 | |
D | ASP683 | |
E | ASP683 | |
F | ASP683 | |
G | ASP683 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 641 |
Chain | Residue | Details |
H | HIS686 | metal ligand |
H | GLU687 | proton acceptor, proton donor |
H | HIS690 | metal ligand |
H | TYR728 | electrostatic stabiliser |
H | GLU735 | metal ligand |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 641 |
Chain | Residue | Details |
I | HIS686 | metal ligand |
I | GLU687 | proton acceptor, proton donor |
I | HIS690 | metal ligand |
I | TYR728 | electrostatic stabiliser |
I | GLU735 | metal ligand |
site_id | MCSA3 |
Number of Residues | 5 |
Details | M-CSA 641 |
Chain | Residue | Details |
J | HIS686 | metal ligand |
J | GLU687 | proton acceptor, proton donor |
J | HIS690 | metal ligand |
J | TYR728 | electrostatic stabiliser |
J | GLU735 | metal ligand |