6VRA
Anthrax octamer prechannel bound to full-length edema factor
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 | 0003824 | molecular_function | catalytic activity |
I | 0004016 | molecular_function | adenylate cyclase activity |
I | 0005515 | molecular_function | protein binding |
I | 0005516 | molecular_function | calmodulin binding |
I | 0005524 | molecular_function | ATP binding |
I | 0005576 | cellular_component | extracellular region |
I | 0006171 | biological_process | cAMP biosynthetic process |
I | 0008237 | molecular_function | metallopeptidase activity |
I | 0008294 | molecular_function | calcium- and calmodulin-responsive adenylate cyclase activity |
I | 0016829 | molecular_function | lyase activity |
I | 0030430 | cellular_component | host cell cytoplasm |
I | 0035821 | biological_process | modulation of process of another organism |
I | 0036094 | molecular_function | small molecule binding |
I | 0044164 | cellular_component | host cell cytosol |
I | 0046872 | molecular_function | metal ion binding |
I | 0090729 | molecular_function | toxin activity |
I | 0099004 | biological_process | obsolete calmodulin dependent kinase signaling pathway |
I | 1902494 | cellular_component | catalytic complex |
J | 0003824 | molecular_function | catalytic activity |
J | 0004016 | molecular_function | adenylate cyclase activity |
J | 0005515 | molecular_function | protein binding |
J | 0005516 | molecular_function | calmodulin binding |
J | 0005524 | molecular_function | ATP binding |
J | 0005576 | cellular_component | extracellular region |
J | 0006171 | biological_process | cAMP biosynthetic process |
J | 0008237 | molecular_function | metallopeptidase activity |
J | 0008294 | molecular_function | calcium- and calmodulin-responsive adenylate cyclase activity |
J | 0016829 | molecular_function | lyase activity |
J | 0030430 | cellular_component | host cell cytoplasm |
J | 0035821 | biological_process | modulation of process of another organism |
J | 0036094 | molecular_function | small molecule binding |
J | 0044164 | cellular_component | host cell cytosol |
J | 0046872 | molecular_function | metal ion binding |
J | 0090729 | molecular_function | toxin activity |
J | 0099004 | biological_process | obsolete calmodulin dependent kinase signaling pathway |
J | 1902494 | cellular_component | catalytic complex |
K | 0003824 | molecular_function | catalytic activity |
K | 0004016 | molecular_function | adenylate cyclase activity |
K | 0005515 | molecular_function | protein binding |
K | 0005516 | molecular_function | calmodulin binding |
K | 0005524 | molecular_function | ATP binding |
K | 0005576 | cellular_component | extracellular region |
K | 0006171 | biological_process | cAMP biosynthetic process |
K | 0008237 | molecular_function | metallopeptidase activity |
K | 0008294 | molecular_function | calcium- and calmodulin-responsive adenylate cyclase activity |
K | 0016829 | molecular_function | lyase activity |
K | 0030430 | cellular_component | host cell cytoplasm |
K | 0035821 | biological_process | modulation of process of another organism |
K | 0036094 | molecular_function | small molecule binding |
K | 0044164 | cellular_component | host cell cytosol |
K | 0046872 | molecular_function | metal ion binding |
K | 0090729 | molecular_function | toxin activity |
K | 0099004 | biological_process | obsolete calmodulin dependent kinase signaling pathway |
K | 1902494 | cellular_component | catalytic complex |
L | 0003824 | molecular_function | catalytic activity |
L | 0004016 | molecular_function | adenylate cyclase activity |
L | 0005515 | molecular_function | protein binding |
L | 0005516 | molecular_function | calmodulin binding |
L | 0005524 | molecular_function | ATP binding |
L | 0005576 | cellular_component | extracellular region |
L | 0006171 | biological_process | cAMP biosynthetic process |
L | 0008237 | molecular_function | metallopeptidase activity |
L | 0008294 | molecular_function | calcium- and calmodulin-responsive adenylate cyclase activity |
L | 0016829 | molecular_function | lyase activity |
L | 0030430 | cellular_component | host cell cytoplasm |
L | 0035821 | biological_process | modulation of process of another organism |
L | 0036094 | molecular_function | small molecule binding |
L | 0044164 | cellular_component | host cell cytosol |
L | 0046872 | molecular_function | metal ion binding |
L | 0090729 | molecular_function | toxin activity |
L | 0099004 | biological_process | obsolete calmodulin dependent kinase signaling pathway |
L | 1902494 | cellular_component | catalytic complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue CA A 801 |
Chain | Residue |
A | ASP177 |
A | ASP179 |
A | ASP181 |
A | ILE183 |
A | GLU188 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 802 |
Chain | Residue |
A | LYS225 |
A | ASP235 |
A | ASP179 |
A | ASP181 |
A | GLU188 |
A | SER222 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue CA B 801 |
Chain | Residue |
B | ASP177 |
B | ASP179 |
B | ASP181 |
B | ILE183 |
B | GLU188 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CA B 802 |
Chain | Residue |
B | ASP179 |
B | ASP181 |
B | GLU188 |
B | SER222 |
B | LYS225 |
B | ASP235 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue CA C 801 |
Chain | Residue |
C | ASP177 |
C | ASP179 |
C | ASP181 |
C | ILE183 |
C | GLU188 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue CA C 802 |
Chain | Residue |
C | ASP179 |
C | ASP181 |
C | GLU188 |
C | SER222 |
C | LYS225 |
C | ASP235 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue CA D 801 |
Chain | Residue |
D | ASP177 |
D | ASP179 |
D | ASP181 |
D | ILE183 |
D | GLU188 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue CA D 802 |
Chain | Residue |
D | ASP179 |
D | ASP181 |
D | GLU188 |
D | SER222 |
D | LYS225 |
D | ASP235 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue CA E 801 |
Chain | Residue |
E | ASP177 |
E | ASP179 |
E | ASP181 |
E | ILE183 |
E | GLU188 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue CA E 802 |
Chain | Residue |
E | ASP179 |
E | ASP181 |
E | GLU188 |
E | SER222 |
E | LYS225 |
E | ASP235 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue CA F 801 |
Chain | Residue |
F | ASP177 |
F | ASP179 |
F | ASP181 |
F | ILE183 |
F | GLU188 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue CA F 802 |
Chain | Residue |
F | ASP179 |
F | ASP181 |
F | GLU188 |
F | SER222 |
F | LYS225 |
F | ASP235 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue CA G 801 |
Chain | Residue |
G | ASP177 |
G | ASP179 |
G | ASP181 |
G | ILE183 |
G | GLU188 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue CA G 802 |
Chain | Residue |
G | ASP179 |
G | ASP181 |
G | GLU188 |
G | SER222 |
G | LYS225 |
G | ASP235 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue CA H 801 |
Chain | Residue |
H | ASP177 |
H | ASP179 |
H | ASP181 |
H | ILE183 |
H | GLU188 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue CA H 802 |
Chain | Residue |
H | ASP179 |
H | ASP181 |
H | GLU188 |
H | SER222 |
H | LYS225 |
H | ASP235 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:11807546 |
Chain | Residue | Details |
I | HIS318 | |
J | HIS318 | |
K | HIS318 | |
L | HIS318 | |
F | GLU302-PHE313 | |
F | ILE316-SER325 | |
H | GLU302-PHE313 | |
H | ILE316-SER325 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15719022, ECO:0007744|PDB:1XFU, ECO:0007744|PDB:1XFV, ECO:0007744|PDB:1XFW, ECO:0007744|PDB:1XFX, ECO:0007744|PDB:1XFY, ECO:0007744|PDB:1XFZ, ECO:0007744|PDB:1Y0V |
Chain | Residue | Details |
I | ASP458 | |
L | ASP458 | |
L | ASP460 | |
L | HIS544 | |
I | ASP460 | |
I | HIS544 | |
J | ASP458 | |
J | ASP460 | |
J | HIS544 | |
K | ASP458 | |
K | ASP460 | |
K | HIS544 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15719022, ECO:0007744|PDB:1XFW |
Chain | Residue | Details |
I | THR515 | |
J | THR515 | |
K | THR515 | |
L | THR515 |
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 |
B | GLU188 | |
D | GLU188 | |
F | GLU188 | |
H | 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 |
B | SER222 | |
B | LYS225 | |
D | SER222 | |
D | LYS225 | |
F | SER222 | |
F | LYS225 | |
H | SER222 | |
H | 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 |
B | ASP235 | |
D | ASP235 | |
F | ASP235 | |
H | ASP235 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | SITE: Cleavage; by FURIN => ECO:0000269|PubMed:11207581, ECO:0000269|PubMed:1438214, ECO:0000269|PubMed:1644824 |
Chain | Residue | Details |
B | GLY167 | |
D | GLY167 | |
F | GLY167 | |
H | GLY167 |
site_id | SWS_FT_FI8 |
Number of Residues | 16 |
Details | SITE: Alpha-clamp => ECO:0000269|PubMed:21037566 |
Chain | Residue | Details |
B | ARG178 | |
F | LEU187 | |
F | PHE236 | |
F | PHE464 | |
H | ARG178 | |
H | LEU187 | |
H | PHE236 | |
H | PHE464 | |
B | LEU187 | |
B | PHE236 | |
B | PHE464 | |
D | ARG178 | |
D | LEU187 | |
D | PHE236 | |
D | PHE464 | |
F | ARG178 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | SITE: Cleavage; by chymotrypsin; required for translocation of LF and EF => ECO:0000269|PubMed:7961869 |
Chain | Residue | Details |
B | PHE314 | |
D | PHE314 | |
F | PHE314 | |
H | PHE314 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | SITE: Phi-clamp => ECO:0000269|PubMed:16051798, ECO:0000269|PubMed:25778700 |
Chain | Residue | Details |
B | PHE427 | |
D | PHE427 | |
F | PHE427 | |
H | PHE427 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | SITE: Essential for binding to cell receptor => ECO:0000269|PubMed:12771151 |
Chain | Residue | Details |
B | ASP683 | |
D | ASP683 | |
F | ASP683 | |
H | ASP683 |