7O85

Anthrax toxin prepore in complex with the neutralizing Fab cAb29

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0051260	biological_process	protein homooligomerization
B	0050825	molecular_function	ice binding
D	0005576	cellular_component	extracellular region
D	0051260	biological_process	protein homooligomerization
E	0050825	molecular_function	ice binding
G	0005576	cellular_component	extracellular region
G	0051260	biological_process	protein homooligomerization
H	0050825	molecular_function	ice binding
J	0005576	cellular_component	extracellular region
J	0051260	biological_process	protein homooligomerization
K	0050825	molecular_function	ice binding
M	0005576	cellular_component	extracellular region
M	0051260	biological_process	protein homooligomerization
N	0050825	molecular_function	ice binding
P	0005576	cellular_component	extracellular region
P	0051260	biological_process	protein homooligomerization
Q	0050825	molecular_function	ice binding
S	0005576	cellular_component	extracellular region
S	0051260	biological_process	protein homooligomerization
T	0050825	molecular_function	ice binding

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
M	ILE316-SER325
P	GLU302-PHE313
P	ILE316-SER325
S	GLU302-PHE313
S	ILE316-SER325
A	ILE316-SER325
D	GLU302-PHE313
D	ILE316-SER325
G	GLU302-PHE313
G	ILE316-SER325
J	GLU302-PHE313
J	ILE316-SER325
M	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
J	ASP177
J	ASP181
J	ILE183
M	ASP177
M	ASP181
M	ILE183
P	ASP177
P	ASP181
P	ILE183
S	ASP177
A	ASP181
S	ASP181
S	ILE183
A	ILE183
D	ASP177
D	ASP181
D	ILE183
G	ASP177
G	ASP181
G	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
D	ASP179
G	ASP179
J	ASP179
M	ASP179
P	ASP179
S	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
D	GLU188
G	GLU188
J	GLU188
M	GLU188
P	GLU188
S	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
M	LYS225
P	SER222
P	LYS225
S	SER222
S	LYS225
A	LYS225
D	SER222
D	LYS225
G	SER222
G	LYS225
J	SER222
J	LYS225
M	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
D	ASP235
G	ASP235
J	ASP235
M	ASP235
P	ASP235
S	ASP235

---

site_id	SWS_FT_FI7
Number of Residues	28
Details	SITE: Alpha-clamp => ECO:0000269|PubMed:21037566

Chain	Residue	Details
A	ARG178
G	LEU187
G	PHE236
G	PHE464
J	ARG178
J	LEU187
J	PHE236
J	PHE464
M	ARG178
M	LEU187
M	PHE236
A	LEU187
M	PHE464
P	ARG178
P	LEU187
P	PHE236
P	PHE464
S	ARG178
S	LEU187
S	PHE236
S	PHE464
A	PHE236
A	PHE464
D	ARG178
D	LEU187
D	PHE236
D	PHE464
G	ARG178

---

site_id	SWS_FT_FI8
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
D	PHE314
G	PHE314
J	PHE314
M	PHE314
P	PHE314
S	PHE314

---

site_id	SWS_FT_FI9
Number of Residues	7
Details	SITE: Phi-clamp => ECO:0000269|PubMed:16051798, ECO:0000269|PubMed:25778700

Chain	Residue	Details
A	PHE427
D	PHE427
G	PHE427
J	PHE427
M	PHE427
P	PHE427
S	PHE427

---