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

---