Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4TSN

Crystal structure of FraC with POC bound (crystal form II)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0006811	biological_process	monoatomic ion transport
A	0006812	biological_process	monoatomic cation transport
A	0008289	molecular_function	lipid binding
A	0015267	molecular_function	channel activity
A	0016020	cellular_component	membrane
A	0031640	biological_process	killing of cells of another organism
A	0035821	biological_process	modulation of process of another organism
A	0042151	cellular_component	nematocyst
A	0042802	molecular_function	identical protein binding
A	0044218	cellular_component	other organism cell membrane
A	0046930	cellular_component	pore complex
A	0046931	biological_process	pore complex assembly
A	0051715	biological_process	cytolysis in another organism
A	0055085	biological_process	transmembrane transport
A	0090729	molecular_function	toxin activity
B	0005576	cellular_component	extracellular region
B	0006811	biological_process	monoatomic ion transport
B	0006812	biological_process	monoatomic cation transport
B	0008289	molecular_function	lipid binding
B	0015267	molecular_function	channel activity
B	0016020	cellular_component	membrane
B	0031640	biological_process	killing of cells of another organism
B	0035821	biological_process	modulation of process of another organism
B	0042151	cellular_component	nematocyst
B	0042802	molecular_function	identical protein binding
B	0044218	cellular_component	other organism cell membrane
B	0046930	cellular_component	pore complex
B	0046931	biological_process	pore complex assembly
B	0051715	biological_process	cytolysis in another organism
B	0055085	biological_process	transmembrane transport
B	0090729	molecular_function	toxin activity
C	0005576	cellular_component	extracellular region
C	0006811	biological_process	monoatomic ion transport
C	0006812	biological_process	monoatomic cation transport
C	0008289	molecular_function	lipid binding
C	0015267	molecular_function	channel activity
C	0016020	cellular_component	membrane
C	0031640	biological_process	killing of cells of another organism
C	0035821	biological_process	modulation of process of another organism
C	0042151	cellular_component	nematocyst
C	0042802	molecular_function	identical protein binding
C	0044218	cellular_component	other organism cell membrane
C	0046930	cellular_component	pore complex
C	0046931	biological_process	pore complex assembly
C	0051715	biological_process	cytolysis in another organism
C	0055085	biological_process	transmembrane transport
C	0090729	molecular_function	toxin activity
D	0005576	cellular_component	extracellular region
D	0006811	biological_process	monoatomic ion transport
D	0006812	biological_process	monoatomic cation transport
D	0008289	molecular_function	lipid binding
D	0015267	molecular_function	channel activity
D	0016020	cellular_component	membrane
D	0031640	biological_process	killing of cells of another organism
D	0035821	biological_process	modulation of process of another organism
D	0042151	cellular_component	nematocyst
D	0042802	molecular_function	identical protein binding
D	0044218	cellular_component	other organism cell membrane
D	0046930	cellular_component	pore complex
D	0046931	biological_process	pore complex assembly
D	0051715	biological_process	cytolysis in another organism
D	0055085	biological_process	transmembrane transport
D	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue PC A 201

Chain	Residue
A	SER54
A	TYR138
A	HOH303
A	HOH318
A	HOH348
A	THR84
A	GLY85
A	SER105
A	PRO107
A	TYR108
A	TYR113
A	TYR133
A	TYR137

site_id	AC2
Number of Residues	7
Details	binding site for residue PC A 202

Chain	Residue
A	TYR113
A	SER114
A	TRP116
A	TYR137
A	PRO142
A	GOL206
A	HOH304

site_id	AC3
Number of Residues	2
Details	binding site for residue PC A 203

Chain	Residue
A	TRP112
A	TYR113

site_id	AC4
Number of Residues	5
Details	binding site for residue SO4 A 204

Chain	Residue
A	ARG120
A	TYR122
A	LYS123
A	HOH366
A	HOH401

site_id	AC5
Number of Residues	5
Details	binding site for residue SO4 A 205

Chain	Residue
A	LYS30
A	ARG31
A	HOH305
A	HOH377
A	HOH454

site_id	AC6
Number of Residues	6
Details	binding site for residue GOL A 206

Chain	Residue
A	TRP112
A	TYR113
A	SER114
A	ARG144
A	PC202
A	HOH302

site_id	AC7
Number of Residues	14
Details	binding site for residue PC B 201

Chain	Residue
B	ARG53
B	SER54
B	THR84
B	GLY85
B	SER105
B	PRO107
B	TYR108
B	TYR113
B	TYR133
B	TYR137
B	TYR138
B	HOH302
B	HOH325
B	HOH352

site_id	AC8
Number of Residues	6
Details	binding site for residue PC B 202

Chain	Residue
B	TYR113
B	SER114
B	TRP116
B	TYR137
B	HOH311
B	HOH394

site_id	AC9
Number of Residues	8
Details	binding site for residue SO4 B 203

Chain	Residue
A	LYS30
A	TYR108
A	HOH307
B	ARG120
B	TYR122
B	LYS123
B	HOH303
B	HOH313

site_id	AD1
Number of Residues	4
Details	binding site for residue SO4 B 204

Chain	Residue
B	ARG144
B	HOH439
D	GLY124
D	GLN125

site_id	AD2
Number of Residues	3
Details	binding site for residue ACT B 205

Chain	Residue
A	ASP109
A	TRP112
B	LYS123

site_id	AD3
Number of Residues	14
Details	binding site for residue PC C 201

Chain	Residue
C	ARG53
C	SER54
C	GLY85
C	SER105
C	PRO107
C	TYR108
C	TYR113
C	TYR133
C	TYR137
C	TYR138
C	SO4202
C	HOH301
C	HOH311
C	HOH351

site_id	AD4
Number of Residues	5
Details	binding site for residue SO4 C 202

Chain	Residue
C	ARG53
C	GLN130
C	TYR133
C	TYR138
C	PC201

site_id	AD5
Number of Residues	9
Details	binding site for residue SO4 C 203

Chain	Residue
C	HOH377
D	HOH334
C	VAL29
C	LYS30
C	LYS77
C	ARG79
C	GLY80
C	HOH303
C	HOH306

site_id	AD6
Number of Residues	5
Details	binding site for residue SO4 C 204

Chain	Residue
C	ARG120
C	TYR122
C	LYS123
C	HOH413
C	HOH441

site_id	AD7
Number of Residues	14
Details	binding site for residue PC D 201

Chain	Residue
D	ARG53
D	SER54
D	GLY85
D	SER105
D	PRO107
D	TYR108
D	TYR113
D	TYR133
D	TYR137
D	TYR138
D	SO4203
D	HOH304
D	HOH330
D	HOH372

site_id	AD8
Number of Residues	7
Details	binding site for residue PC D 202

Chain	Residue
D	TRP112
D	TYR113
D	SER114
D	TRP116
D	TYR137
D	PRO142
D	HOH390

site_id	AD9
Number of Residues	5
Details	binding site for residue SO4 D 203

Chain	Residue
D	ARG53
D	GLN130
D	TYR133
D	TYR138
D	PC201

site_id	AE1
Number of Residues	8
Details	binding site for residue SO4 D 204

Chain	Residue
D	ASN28
D	VAL29
D	LYS30
D	LYS77
D	ARG79
D	GLY80
D	HOH337
D	HOH343

site_id	AE2
Number of Residues	6
Details	binding site for residue SO4 D 205

Chain	Residue
B	THR56
B	ASN78
B	ARG79
D	SER167
D	HOH318
D	HOH336

site_id	AE3
Number of Residues	5
Details	binding site for residue SO4 D 206

Chain	Residue
C	ARG79
D	ARG120
D	TYR122
D	LYS123
D	HOH405

site_id	AE4
Number of Residues	1
Details	binding site for residue SO4 D 207

Chain	Residue
D	LYS178

site_id	AE5
Number of Residues	2
Details	binding site for residue ACT D 208

Chain	Residue
D	ASN28
D	ARG79

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	60
Details	Region: {"description":"Trp-rich region, which is important for the binding to lipid membrane","evidences":[{"source":"UniProtKB","id":"P61914","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Motif: {"description":"Cell attachment site, crucial for protein stability","evidences":[{"source":"UniProtKB","id":"P07845","evidenceCode":"ECO:0000250"},{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"description":"in subunit A; in oligomeric forms only","evidences":[{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"28630155","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	36
Details	Binding site: {"description":"in monomeric and oligomeric forms","evidences":[{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"description":"in subunit B; in oligomeric forms only","evidences":[{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Site: {"description":"Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B); essential in hemolysis, since it is critical for pore formation in cholesterol-rich membrane cells (such as red blood cells)","evidences":[{"source":"PubMed","id":"21300287","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25759390","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Site: {"description":"Protrudes from one subunit (B) and inserts into the hydrophobic cavity from the adjacent subunit (A)","evidences":[{"source":"PubMed","id":"21300287","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Site: {"description":"Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B)","evidences":[{"source":"PubMed","id":"21300287","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Site: {"description":"Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B)","evidences":[{"source":"PubMed","id":"21300287","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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