Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5EC5

Crystal structure of lysenin pore

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
B	0005576	cellular_component	extracellular region
C	0005576	cellular_component	extracellular region
D	0005576	cellular_component	extracellular region
E	0005576	cellular_component	extracellular region
F	0005576	cellular_component	extracellular region
G	0005576	cellular_component	extracellular region
H	0005576	cellular_component	extracellular region
I	0005576	cellular_component	extracellular region
J	0005576	cellular_component	extracellular region
K	0005576	cellular_component	extracellular region
L	0005576	cellular_component	extracellular region
M	0005576	cellular_component	extracellular region
N	0005576	cellular_component	extracellular region
O	0005576	cellular_component	extracellular region
P	0005576	cellular_component	extracellular region
R	0005576	cellular_component	extracellular region
S	0005576	cellular_component	extracellular region

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue MBO A 301

Chain	Residue
A	SER226
A	ASP228
A	PHE266
A	SER269
A	CYS283
A	ASP285

site_id	AC2
Number of Residues	6
Details	binding site for residue MBO A 302

Chain	Residue
A	LEU284
A	ARG287
B	ARG52
A	CYS272
A	TYR273
A	ASP274

site_id	AC3
Number of Residues	4
Details	binding site for residue MBO B 301

Chain	Residue
B	CYS272
B	TYR273
B	ASP274
B	ARG287

site_id	AC4
Number of Residues	6
Details	binding site for residue MBO B 302

Chain	Residue
B	SER226
B	ASP228
B	PHE266
B	SER269
B	CYS283
B	ASP285

site_id	AC5
Number of Residues	6
Details	binding site for residue MBO C 301

Chain	Residue
C	SER226
C	ASP228
C	PHE266
C	SER269
C	CYS283
C	ASP285

site_id	AC6
Number of Residues	3
Details	binding site for residue HG C 302

Chain	Residue
C	CYS272
C	TYR273
C	ARG287

site_id	AC7
Number of Residues	6
Details	binding site for residue MBO D 301

Chain	Residue
D	SER226
D	ASP228
D	PHE266
D	SER269
D	CYS283
D	ASP285

site_id	AC8
Number of Residues	3
Details	binding site for residue HG D 302

Chain	Residue
D	CYS272
D	TYR273
D	ARG287

site_id	AC9
Number of Residues	6
Details	binding site for residue MBO E 301

Chain	Residue
E	SER226
E	ASP228
E	PHE266
E	SER269
E	CYS283
E	ASP285

site_id	AD1
Number of Residues	5
Details	binding site for residue HG E 302

Chain	Residue
E	CYS272
E	TYR273
E	ASP274
E	LEU284
E	ARG287

site_id	AD2
Number of Residues	5
Details	binding site for residue HG F 301

Chain	Residue
F	CYS272
F	TYR273
F	ASP274
F	LEU284
F	ARG287

site_id	AD3
Number of Residues	7
Details	binding site for residue MBO F 302

Chain	Residue
F	SER226
F	ASP228
F	GLN229
F	GLY230
F	PHE266
F	SER269
F	CYS283

site_id	AD4
Number of Residues	8
Details	binding site for residue MBO G 301

Chain	Residue
G	SER226
G	SER227
G	ASP228
G	GLY230
G	PHE266
G	SER269
G	CYS283
G	ASP285

site_id	AD5
Number of Residues	3
Details	binding site for residue HG G 302

Chain	Residue
G	CYS272
G	TYR273
G	LEU284

site_id	AD6
Number of Residues	5
Details	binding site for residue MBO H 301

Chain	Residue
H	CYS272
H	TYR273
H	ASP274
H	LEU284
H	ARG287

site_id	AD7
Number of Residues	4
Details	binding site for residue MBO H 302

Chain	Residue
H	SER226
H	PHE266
H	SER269
H	CYS283

site_id	AD8
Number of Residues	5
Details	binding site for residue HG I 301

Chain	Residue
I	CYS272
I	TYR273
I	ASP274
I	LEU284
I	ARG287

site_id	AD9
Number of Residues	6
Details	binding site for residue MBO I 302

Chain	Residue
I	SER226
I	SER227
I	ASP228
I	PHE266
I	SER269
I	CYS283

site_id	AE1
Number of Residues	3
Details	binding site for residue HG J 301

Chain	Residue
J	SER226
J	SER269
J	CYS283

site_id	AE2
Number of Residues	4
Details	binding site for residue HG J 302

Chain	Residue
J	ASP274
J	ARG287
J	CYS272
J	TYR273

site_id	AE3
Number of Residues	8
Details	binding site for residue MBO K 301

Chain	Residue
K	SER226
K	SER227
K	ASP228
K	PHE266
K	SER269
K	CYS283
K	ASP285
K	HOH406

site_id	AE4
Number of Residues	5
Details	binding site for residue MBO K 302

Chain	Residue
K	CYS272
K	TYR273
K	ASP274
K	LEU284
K	ARG287

site_id	AE5
Number of Residues	6
Details	binding site for residue MBO L 301

Chain	Residue
L	SER226
L	ASP228
L	PHE266
L	SER269
L	CYS283
L	ASP285

site_id	AE6
Number of Residues	4
Details	binding site for residue MBO L 302

Chain	Residue
L	CYS272
L	TYR273
L	ASP274
L	ARG287

site_id	AE7
Number of Residues	6
Details	binding site for residue MBO M 301

Chain	Residue
M	SER226
M	ASP228
M	GLY230
M	PHE266
M	SER269
M	CYS283

site_id	AE8
Number of Residues	6
Details	binding site for residue MBO M 302

Chain	Residue
L	ARG52
M	CYS272
M	TYR273
M	ASP274
M	LEU284
M	ARG287

site_id	AE9
Number of Residues	3
Details	binding site for residue HG N 301

Chain	Residue
N	SER226
N	SER269
N	CYS283

site_id	AF1
Number of Residues	5
Details	binding site for residue HG N 302

Chain	Residue
N	CYS272
N	TYR273
N	ASP274
N	LEU284
N	ARG287

site_id	AF2
Number of Residues	5
Details	binding site for residue MBO O 301

Chain	Residue
O	SER226
O	PHE266
O	SER269
O	CYS283
O	ASP285

site_id	AF3
Number of Residues	2
Details	binding site for residue HG O 302

Chain	Residue
O	CYS272
O	TYR273

site_id	AF4
Number of Residues	2
Details	binding site for residue HG P 301

Chain	Residue
P	CYS272
P	TYR273

site_id	AF5
Number of Residues	6
Details	binding site for residue MBO P 302

Chain	Residue
P	SER226
P	ASP228
P	GLY230
P	PHE266
P	SER269
P	CYS283

site_id	AF6
Number of Residues	7
Details	binding site for residue MBO R 301

Chain	Residue
R	SER226
R	SER227
R	ASP228
R	GLY230
R	PHE266
R	SER269
R	CYS283

site_id	AF7
Number of Residues	3
Details	binding site for residue HG R 302

Chain	Residue
R	CYS272
R	TYR273
R	ARG287

site_id	AF8
Number of Residues	6
Details	binding site for residue MBO S 301

Chain	Residue
S	SER226
S	ASP228
S	PHE266
S	SER269
S	CYS283
S	ASP285

site_id	AF9
Number of Residues	5
Details	binding site for residue HG S 302

Chain	Residue
S	CYS272
S	TYR273
S	ASP274
S	LEU284
S	ARG287

Functional Information from PROSITE/UniProt

site_id	PS00435
Number of Residues	11
Details	PEROXIDASE_1 Peroxidases proximal heme-ligand signature. ETRTVTATHSI

Chain	Residue	Details
A	GLU50-ILE60

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1278
Details	Region: {"description":"N-terminal cap domain","evidences":[{"source":"PubMed","id":"27048994","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	584
Details	Region: {"description":"Beta-hairpin domain","evidences":[{"source":"PubMed","id":"27048994","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2520
Details	Region: {"description":"C-terminal receptor-binding domain","evidences":[{"source":"PubMed","id":"27048994","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	72
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22819216","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	54
Details	Site: {"description":"Crucial for binding sphingomyelin and inducing hemolysis","evidences":[{"source":"PubMed","id":"15274631","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	18
Details	Site: {"description":"Crucial for binding sphingomyelin and important for inducing hemolysis","evidences":[{"source":"PubMed","id":"15274631","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	18
Details	Site: {"description":"Important for activity"}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)