6UJI
Low resolution crystal structure (5.5 A) of the anthrax toxin protective antigen heptamer prepore D425A mutant
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 | 0005576 | cellular_component | extracellular region |
H | 0051260 | biological_process | protein homooligomerization |
I | 0005576 | cellular_component | extracellular region |
I | 0051260 | biological_process | protein homooligomerization |
J | 0005576 | cellular_component | extracellular region |
J | 0051260 | biological_process | protein homooligomerization |
K | 0005576 | cellular_component | extracellular region |
K | 0051260 | biological_process | protein homooligomerization |
L | 0005576 | cellular_component | extracellular region |
L | 0051260 | biological_process | protein homooligomerization |
M | 0005576 | cellular_component | extracellular region |
M | 0051260 | biological_process | protein homooligomerization |
N | 0005576 | cellular_component | extracellular region |
N | 0051260 | biological_process | protein homooligomerization |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 280 |
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 | |
H | GLU302-PHE313 | |
H | ILE316-SER325 | |
I | GLU302-PHE313 | |
I | ILE316-SER325 | |
J | GLU302-PHE313 | |
A | ILE316-SER325 | |
J | ILE316-SER325 | |
K | GLU302-PHE313 | |
K | ILE316-SER325 | |
L | GLU302-PHE313 | |
L | ILE316-SER325 | |
M | GLU302-PHE313 | |
M | ILE316-SER325 | |
N | GLU302-PHE313 | |
N | 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 | 42 |
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 | |
H | ASP177 | |
H | ASP181 | |
H | ILE183 | |
I | ASP177 | |
I | ASP181 | |
I | ILE183 | |
J | ASP177 | |
J | ASP181 | |
A | ILE183 | |
J | ILE183 | |
K | ASP177 | |
K | ASP181 | |
K | ILE183 | |
L | ASP177 | |
L | ASP181 | |
L | ILE183 | |
M | ASP177 | |
M | ASP181 | |
M | ILE183 | |
B | ASP177 | |
N | ASP177 | |
N | ASP181 | |
N | ILE183 | |
B | ASP181 | |
B | ILE183 | |
C | ASP177 | |
C | ASP181 | |
C | ILE183 |
site_id | SWS_FT_FI3 |
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: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 | |
J | ASP179 | |
K | ASP179 | |
L | ASP179 | |
M | ASP179 | |
N | ASP179 | |
B | ASP179 | |
C | ASP179 | |
D | ASP179 | |
E | ASP179 | |
F | ASP179 | |
G | ASP179 | |
H | ASP179 | |
I | ASP179 |
site_id | SWS_FT_FI4 |
Number of Residues | 14 |
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 | |
J | GLU188 | |
K | GLU188 | |
L | GLU188 | |
M | GLU188 | |
N | GLU188 | |
B | GLU188 | |
C | GLU188 | |
D | GLU188 | |
E | GLU188 | |
F | GLU188 | |
G | GLU188 | |
H | GLU188 | |
I | GLU188 |
site_id | SWS_FT_FI5 |
Number of Residues | 28 |
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 | |
H | SER222 | |
H | LYS225 | |
I | SER222 | |
I | LYS225 | |
J | SER222 | |
A | LYS225 | |
J | LYS225 | |
K | SER222 | |
K | LYS225 | |
L | SER222 | |
L | LYS225 | |
M | SER222 | |
M | LYS225 | |
N | SER222 | |
N | LYS225 | |
B | SER222 | |
B | LYS225 | |
C | SER222 | |
C | LYS225 | |
D | SER222 | |
D | LYS225 | |
E | SER222 |
site_id | SWS_FT_FI6 |
Number of Residues | 14 |
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 | |
J | ASP235 | |
K | ASP235 | |
L | ASP235 | |
M | ASP235 | |
N | ASP235 | |
B | ASP235 | |
C | ASP235 | |
D | ASP235 | |
E | ASP235 | |
F | ASP235 | |
G | ASP235 | |
H | ASP235 | |
I | ASP235 |
site_id | SWS_FT_FI7 |
Number of Residues | 56 |
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 | |
H | ARG178 | |
A | PHE236 | |
H | LEU187 | |
H | PHE236 | |
H | PHE464 | |
I | ARG178 | |
I | LEU187 | |
I | PHE236 | |
I | PHE464 | |
J | ARG178 | |
J | LEU187 | |
J | PHE236 | |
A | PHE464 | |
J | PHE464 | |
K | ARG178 | |
K | LEU187 | |
K | PHE236 | |
K | PHE464 | |
L | ARG178 | |
L | LEU187 | |
L | PHE236 | |
L | PHE464 | |
M | ARG178 | |
B | ARG178 | |
M | LEU187 | |
M | PHE236 | |
M | PHE464 | |
N | ARG178 | |
N | LEU187 | |
N | PHE236 | |
N | PHE464 | |
B | LEU187 | |
B | PHE236 | |
B | PHE464 | |
C | ARG178 |
site_id | SWS_FT_FI8 |
Number of Residues | 14 |
Details | SITE: Cleavage; by chymotrypsin; required for translocation of LF and EF => ECO:0000269|PubMed:7961869 |
Chain | Residue | Details |
A | PHE314 | |
J | PHE314 | |
K | PHE314 | |
L | PHE314 | |
M | PHE314 | |
N | PHE314 | |
B | PHE314 | |
C | PHE314 | |
D | PHE314 | |
E | PHE314 | |
F | PHE314 | |
G | PHE314 | |
H | PHE314 | |
I | PHE314 |
site_id | SWS_FT_FI9 |
Number of Residues | 14 |
Details | SITE: Phi-clamp => ECO:0000269|PubMed:16051798, ECO:0000269|PubMed:25778700 |
Chain | Residue | Details |
A | PHE427 | |
J | PHE427 | |
K | PHE427 | |
L | PHE427 | |
M | PHE427 | |
N | PHE427 | |
B | PHE427 | |
C | PHE427 | |
D | PHE427 | |
E | PHE427 | |
F | PHE427 | |
G | PHE427 | |
H | PHE427 | |
I | PHE427 |
site_id | SWS_FT_FI10 |
Number of Residues | 14 |
Details | SITE: Essential for binding to cell receptor => ECO:0000269|PubMed:12771151 |
Chain | Residue | Details |
A | ASP683 | |
J | ASP683 | |
K | ASP683 | |
L | ASP683 | |
M | ASP683 | |
N | ASP683 | |
B | ASP683 | |
C | ASP683 | |
D | ASP683 | |
E | ASP683 | |
F | ASP683 | |
G | ASP683 | |
H | ASP683 | |
I | ASP683 |