3KWV
Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers
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 | 0003824 | molecular_function | catalytic activity |
C | 0005576 | cellular_component | extracellular region |
C | 0008237 | molecular_function | metallopeptidase activity |
C | 0046872 | molecular_function | metal ion binding |
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 | 0003824 | molecular_function | catalytic activity |
F | 0005576 | cellular_component | extracellular region |
F | 0008237 | molecular_function | metallopeptidase activity |
F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 736 |
Chain | Residue |
A | ASP177 |
A | ASP179 |
A | ASP181 |
A | ILE183 |
A | GLU188 |
A | HOH738 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 737 |
Chain | Residue |
A | SER222 |
A | LYS225 |
A | ASP235 |
A | ASP179 |
A | ASP181 |
A | GLU188 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 736 |
Chain | Residue |
B | ASP177 |
B | ASP179 |
B | ASP181 |
B | ILE183 |
B | GLU188 |
B | HOH738 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 737 |
Chain | Residue |
B | ASP179 |
B | ASP181 |
B | GLU188 |
B | SER222 |
B | LYS225 |
B | ASP235 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA D 736 |
Chain | Residue |
D | ASP177 |
D | ASP179 |
D | ASP181 |
D | ILE183 |
D | GLU188 |
D | HOH738 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA D 737 |
Chain | Residue |
D | ASP179 |
D | ASP181 |
D | GLU188 |
D | SER222 |
D | LYS225 |
D | ASP235 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA E 736 |
Chain | Residue |
E | ASP177 |
E | ASP179 |
E | ASP181 |
E | ILE183 |
E | GLU188 |
E | HOH738 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA E 737 |
Chain | Residue |
E | ASP179 |
E | ASP181 |
E | GLU188 |
E | SER222 |
E | LYS225 |
E | ASP235 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 80 |
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-ALA333 | |
A | HIS336-THR345 | |
B | GLU302-ALA333 | |
B | HIS336-THR345 | |
D | GLU302-ALA333 | |
D | HIS336-THR345 | |
E | GLU302-ALA333 | |
E | HIS336-THR345 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
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 | |
E | ASP177 | |
E | ASP181 | |
E | ILE183 | |
A | ASP181 | |
A | ILE183 | |
B | ASP177 | |
B | ASP181 | |
B | ILE183 | |
D | ASP177 | |
D | ASP181 | |
D | ILE183 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
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 | |
D | ASP179 | |
E | ASP179 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
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 | |
D | GLU188 | |
E | GLU188 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
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 | |
A | LYS225 | |
B | SER222 | |
B | LYS225 | |
D | SER222 | |
D | LYS225 | |
E | SER222 | |
E | LYS225 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
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 | |
D | ASP235 | |
E | ASP235 |
site_id | SWS_FT_FI7 |
Number of Residues | 16 |
Details | SITE: Alpha-clamp => ECO:0000269|PubMed:21037566 |
Chain | Residue | Details |
A | ARG178 | |
D | LEU187 | |
D | PHE236 | |
D | ILE484 | |
E | ARG178 | |
E | LEU187 | |
E | PHE236 | |
E | ILE484 | |
A | LEU187 | |
A | PHE236 | |
A | ILE484 | |
B | ARG178 | |
B | LEU187 | |
B | PHE236 | |
B | ILE484 | |
D | ARG178 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | SITE: Cleavage; by chymotrypsin; required for translocation of LF and EF => ECO:0000269|PubMed:7961869 |
Chain | Residue | Details |
A | ILE334 | |
B | ILE334 | |
D | ILE334 | |
E | ILE334 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | SITE: Phi-clamp => ECO:0000269|PubMed:16051798, ECO:0000269|PubMed:25778700 |
Chain | Residue | Details |
A | GLN447 | |
B | GLN447 | |
D | GLN447 | |
E | GLN447 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | SITE: Essential for binding to cell receptor => ECO:0000269|PubMed:12771151 |
Chain | Residue | Details |
A | LYS703 | |
B | LYS703 | |
D | LYS703 | |
E | LYS703 |