Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6WJJ

Anthrax octamer prechannel bound to full-length 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
H	0005576	cellular_component	extracellular region
H	0051260	biological_process	protein homooligomerization
I	0003824	molecular_function	catalytic activity
I	0004222	molecular_function	metalloendopeptidase activity
I	0005515	molecular_function	protein binding
I	0005576	cellular_component	extracellular region
I	0006508	biological_process	proteolysis
I	0008237	molecular_function	metallopeptidase activity
I	0008270	molecular_function	zinc ion binding
I	0030430	cellular_component	host cell cytoplasm
I	0035821	biological_process	modulation of process of another organism
I	0044164	cellular_component	host cell cytosol
I	0046872	molecular_function	metal ion binding
I	0090729	molecular_function	toxin activity
J	0003824	molecular_function	catalytic activity
J	0004222	molecular_function	metalloendopeptidase activity
J	0005515	molecular_function	protein binding
J	0005576	cellular_component	extracellular region
J	0006508	biological_process	proteolysis
J	0008237	molecular_function	metallopeptidase activity
J	0008270	molecular_function	zinc ion binding
J	0030430	cellular_component	host cell cytoplasm
J	0035821	biological_process	modulation of process of another organism
J	0044164	cellular_component	host cell cytosol
J	0046872	molecular_function	metal ion binding
J	0090729	molecular_function	toxin activity
K	0003824	molecular_function	catalytic activity
K	0004222	molecular_function	metalloendopeptidase activity
K	0005515	molecular_function	protein binding
K	0005576	cellular_component	extracellular region
K	0006508	biological_process	proteolysis
K	0008237	molecular_function	metallopeptidase activity
K	0008270	molecular_function	zinc ion binding
K	0030430	cellular_component	host cell cytoplasm
K	0035821	biological_process	modulation of process of another organism
K	0044164	cellular_component	host cell cytosol
K	0046872	molecular_function	metal ion binding
K	0090729	molecular_function	toxin activity
L	0003824	molecular_function	catalytic activity
L	0004222	molecular_function	metalloendopeptidase activity
L	0005515	molecular_function	protein binding
L	0005576	cellular_component	extracellular region
L	0006508	biological_process	proteolysis
L	0008237	molecular_function	metallopeptidase activity
L	0008270	molecular_function	zinc ion binding
L	0030430	cellular_component	host cell cytoplasm
L	0035821	biological_process	modulation of process of another organism
L	0044164	cellular_component	host cell cytosol
L	0046872	molecular_function	metal ion binding
L	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue CA A 801

Chain	Residue
A	ASP177
A	ASP179
A	ASP181
A	ILE183
A	GLU188
A	CA802

site_id	AC2
Number of Residues	7
Details	binding site for residue CA A 802

Chain	Residue
A	SER222
A	LYS225
A	ASP235
A	CA801
A	ASP179
A	ASP181
A	GLU188

site_id	AC3
Number of Residues	6
Details	binding site for residue CA B 801

Chain	Residue
B	ASP177
B	ASP179
B	ASP181
B	ILE183
B	GLU188
B	CA802

site_id	AC4
Number of Residues	8
Details	binding site for residue CA B 802

Chain	Residue
B	ASP179
B	ASP181
B	GLU188
B	SER221
B	SER222
B	LYS225
B	ASP235
B	CA801

site_id	AC5
Number of Residues	2
Details	binding site for residue SO4 L 801

Chain	Residue
L	ARG267
L	TYR268

site_id	AC6
Number of Residues	1
Details	binding site for residue ZN L 802

Chain	Residue
L	TYR728

site_id	AC7
Number of Residues	6
Details	binding site for residue CA C 801

Chain	Residue
C	ASP177
C	ASP179
C	ASP181
C	ILE183
C	GLU188
C	CA802

site_id	AC8
Number of Residues	7
Details	binding site for residue CA C 802

Chain	Residue
C	ASP179
C	ASP181
C	GLU188
C	SER222
C	LYS225
C	ASP235
C	CA801

site_id	AC9
Number of Residues	6
Details	binding site for residue CA F 801

Chain	Residue
F	ASP177
F	ASP179
F	ASP181
F	ILE183
F	GLU188
F	CA802

site_id	AD1
Number of Residues	8
Details	binding site for residue CA F 802

Chain	Residue
F	ASP179
F	ASP181
F	GLU188
F	SER221
F	SER222
F	LYS225
F	ASP235
F	CA801

site_id	AD2
Number of Residues	2
Details	binding site for residue SO4 I 801

Chain	Residue
I	ARG267
I	TYR268

site_id	AD3
Number of Residues	1
Details	binding site for residue ZN I 802

Chain	Residue
I	TYR728

site_id	AD4
Number of Residues	6
Details	binding site for residue CA D 801

Chain	Residue
D	ASP177
D	ASP179
D	ASP181
D	ILE183
D	GLU188
D	CA802

site_id	AD5
Number of Residues	7
Details	binding site for residue CA D 802

Chain	Residue
D	ASP179
D	ASP181
D	GLU188
D	SER222
D	LYS225
D	ASP235
D	CA801

site_id	AD6
Number of Residues	6
Details	binding site for residue CA G 801

Chain	Residue
G	ASP177
G	ASP179
G	ASP181
G	ILE183
G	GLU188
G	CA802

site_id	AD7
Number of Residues	8
Details	binding site for residue CA G 802

Chain	Residue
G	ASP179
G	ASP181
G	GLU188
G	SER221
G	SER222
G	LYS225
G	ASP235
G	CA801

site_id	AD8
Number of Residues	2
Details	binding site for residue SO4 J 801

Chain	Residue
J	ARG267
J	TYR268

site_id	AD9
Number of Residues	1
Details	binding site for residue ZN J 802

Chain	Residue
J	TYR728

site_id	AE1
Number of Residues	6
Details	binding site for residue CA E 801

Chain	Residue
E	ASP177
E	ASP179
E	ASP181
E	ILE183
E	GLU188
E	CA802

site_id	AE2
Number of Residues	7
Details	binding site for residue CA E 802

Chain	Residue
E	SER222
E	LYS225
E	ASP235
E	CA801
E	ASP179
E	ASP181
E	GLU188

site_id	AE3
Number of Residues	6
Details	binding site for residue CA H 801

Chain	Residue
H	ASP177
H	ASP179
H	ASP181
H	ILE183
H	GLU188
H	CA802

site_id	AE4
Number of Residues	8
Details	binding site for residue CA H 802

Chain	Residue
H	ASP179
H	ASP181
H	GLU188
H	SER221
H	SER222
H	LYS225
H	ASP235
H	CA801

site_id	AE5
Number of Residues	2
Details	binding site for residue SO4 K 801

Chain	Residue
K	ARG267
K	TYR268

site_id	AE6
Number of Residues	1
Details	binding site for residue ZN K 802

Chain	Residue
K	TYR728

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	4
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU01339, ECO:0000269\|PubMed:19651869, ECO:0000269\|PubMed:9573135

Chain	Residue	Details
L	GLU687
I	GLU687
J	GLU687
K	GLU687
G	GLU302-PHE313
G	ILE316-SER325
H	GLU302-PHE313
H	ILE316-SER325

site_id	SWS_FT_FI2
Number of Residues	12
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
K	HIS686
K	HIS690
K	GLU735
L	HIS690
L	GLU735
I	HIS686
I	HIS690
I	GLU735
J	HIS686
J	HIS690
J	GLU735

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01339

Chain	Residue	Details
L	TYR728
I	TYR728
J	TYR728
K	TYR728

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
F	GLU188
G	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
F	SER222
F	LYS225
G	SER222
G	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
F	ASP235
G	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
F	GLY167
G	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
G	LEU187
G	PHE236
G	PHE464
H	ARG178
H	LEU187
H	PHE236
H	PHE464
B	LEU187
B	PHE236
B	PHE464
F	ARG178
F	LEU187
F	PHE236
F	PHE464
G	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
F	PHE314
G	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
F	PHE427
G	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
F	ASP683
G	ASP683
H	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

site_id	MCSA2
Number of Residues	5
Details	M-CSA 641

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

site_id	MCSA3
Number of Residues	5
Details	M-CSA 641

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

site_id	MCSA4
Number of Residues	5
Details	M-CSA 641

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

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