Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6PSN

Anthrax toxin protective antigen channels bound to lethal 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
L	0003824	molecular_function	catalytic activity
L	0005576	cellular_component	extracellular region
L	0008237	molecular_function	metallopeptidase activity
L	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue CA A 801

Chain	Residue
A	ASP179
A	ASP181
A	ILE183
A	ASP185
A	CA802

site_id	AC2
Number of Residues	6
Details	binding site for residue CA A 802

Chain	Residue
A	ASP235
A	CA801
A	ASP179
A	ASP181
A	SER222
A	LYS225

site_id	AC3
Number of Residues	4
Details	binding site for residue CA B 801

Chain	Residue
B	ASP179
B	ASP181
B	ILE183
B	ASP185

site_id	AC4
Number of Residues	5
Details	binding site for residue CA B 802

Chain	Residue
B	ASP179
B	ASP181
B	SER222
B	LYS225
B	ASP235

site_id	AC5
Number of Residues	5
Details	binding site for residue CA C 801

Chain	Residue
C	ASP179
C	ASP181
C	ILE183
C	ASP185
C	CA802

site_id	AC6
Number of Residues	6
Details	binding site for residue CA C 802

Chain	Residue
C	ASP179
C	ASP181
C	SER222
C	LYS225
C	ASP235
C	CA801

site_id	AC7
Number of Residues	4
Details	binding site for residue CA D 801

Chain	Residue
D	ASP179
D	ASP181
D	ILE183
D	ASP185

site_id	AC8
Number of Residues	5
Details	binding site for residue CA D 802

Chain	Residue
D	ASP179
D	ASP181
D	SER222
D	LYS225
D	ASP235

site_id	AC9
Number of Residues	4
Details	binding site for residue CA E 801

Chain	Residue
E	ASP179
E	ASP181
E	ILE183
E	ASP185

site_id	AD1
Number of Residues	5
Details	binding site for residue CA E 802

Chain	Residue
E	ASP179
E	ASP181
E	SER222
E	LYS225
E	ASP235

site_id	AD2
Number of Residues	4
Details	binding site for residue CA F 801

Chain	Residue
F	ASP179
F	ASP181
F	ILE183
F	ASP185

site_id	AD3
Number of Residues	5
Details	binding site for residue CA F 802

Chain	Residue
F	ASP179
F	ASP181
F	SER222
F	LYS225
F	ASP235

site_id	AD4
Number of Residues	4
Details	binding site for residue CA G 801

Chain	Residue
G	ASP179
G	ASP181
G	ILE183
G	ASP185

site_id	AD5
Number of Residues	5
Details	binding site for residue CA G 802

Chain	Residue
G	ASP179
G	ASP181
G	SER222
G	LYS225
G	ASP235

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. GFIHEFGHAV

Chain	Residue	Details
L	GLY683-VAL692

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU01339, ECO:0000269\|PubMed:19651869, ECO:0000269\|PubMed:9573135

Chain	Residue	Details
L	GLU687
E	ILE316-SER325
F	GLU302-PHE313
F	ILE316-SER325
G	GLU302-PHE313
G	ILE316-SER325
A	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	3
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01339, ECO:0000269\|PubMed:11700563, ECO:0000269\|PubMed:14718924, ECO:0000269\|PubMed:14718925, ECO:0000269\|PubMed:15911756, ECO:0000269\|PubMed:22342144, ECO:0000269\|PubMed:25372673, ECO:0000269\|PubMed:26492514, ECO:0000269\|PubMed:26578066, ECO:0007744\|PDB:1J7N, ECO:0007744\|PDB:1PWP, ECO:0007744\|PDB:1PWQ, ECO:0007744\|PDB:1PWU, ECO:0007744\|PDB:1PWW, ECO:0007744\|PDB:1YQY, ECO:0007744\|PDB:4DV8, ECO:0007744\|PDB:4PKQ, ECO:0007744\|PDB:4PKR, ECO:0007744\|PDB:4PKS, ECO:0007744\|PDB:4PKT, ECO:0007744\|PDB:4PKV, ECO:0007744\|PDB:4PKW, ECO:0007744\|PDB:4WF6, ECO:0007744\|PDB:4XM6, ECO:0007744\|PDB:4XM7, ECO:0007744\|PDB:5D1S, ECO:0007744\|PDB:5D1T

Chain	Residue	Details
L	HIS686
D	ASP177
D	ASP181
D	ILE183
E	ASP177
E	ASP181
E	ILE183
F	ASP177
F	ASP181
F	ILE183
G	ASP177
L	HIS690
G	ASP181
G	ILE183
L	GLU735
B	ASP177
B	ASP181
B	ILE183
C	ASP177
C	ASP181
C	ILE183

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01339

Chain	Residue	Details
L	TYR728
B	ASP179
C	ASP179
D	ASP179
E	ASP179
F	ASP179
G	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
B	GLU188
C	GLU188
D	GLU188
E	GLU188
F	GLU188
G	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
E	LYS225
F	SER222
F	LYS225
G	SER222
G	LYS225
A	LYS225
B	SER222
B	LYS225
C	SER222
C	LYS225
D	SER222
D	LYS225
E	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
B	ASP235
C	ASP235
D	ASP235
E	ASP235
F	ASP235
G	ASP235

site_id	SWS_FT_FI7
Number of Residues	28
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
A	PHE236
A	PHE464
B	ARG178
B	LEU187
B	PHE236
B	PHE464
C	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
B	PHE314
C	PHE314
D	PHE314
E	PHE314
F	PHE314
G	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
B	PHE427
C	PHE427
D	PHE427
E	PHE427
F	PHE427
G	PHE427

site_id	SWS_FT_FI10
Number of Residues	7
Details	SITE: Essential for binding to cell receptor => ECO:0000269\|PubMed:12771151

Chain	Residue	Details
A	ASP683
B	ASP683
C	ASP683
D	ASP683
E	ASP683
F	ASP683
G	ASP683

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 641

Chain	Residue	Details
L	HIS686	metal ligand
L	GLU687	proton acceptor, proton donor
L	HIS690	metal ligand
L	TYR728	electrostatic stabiliser
L	GLU735	metal ligand

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)