Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4TSY

Crystal structure of FraC with lipids

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	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	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	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	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	10
Details	binding site for residue HXJ A 201

Chain	Residue
A	ARG53
A	SO4204
A	SER54
A	THR84
A	GLY85
A	PRO107
A	TYR108
A	TYR113
A	TYR133
A	TYR137

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

Chain	Residue
A	ASN111
A	TRP112
A	TYR113
A	SER114
A	TRP116
A	TYR137
A	PRO142

site_id	AC3
Number of Residues	3
Details	binding site for residue SO4 A 203

Chain	Residue
A	ARG120
A	TYR122
A	LYS123

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

Chain	Residue
A	ARG53
A	GLN130
A	TYR133
A	TYR138
A	HXJ201

site_id	AC5
Number of Residues	4
Details	binding site for residue SO4 A 205

Chain	Residue
A	TRP149
A	ARG161
A	HIS175
B	HIS63

site_id	AC6
Number of Residues	4
Details	binding site for residue SO4 A 206

Chain	Residue
A	THR44
A	SER95
A	HTO209
C	LYS123

site_id	AC7
Number of Residues	2
Details	binding site for residue SO4 A 207

Chain	Residue
A	ARG79
D	HIS169

site_id	AC8
Number of Residues	2
Details	binding site for residue SO4 A 208

Chain	Residue
A	TYR51
A	ARG53

site_id	AC9
Number of Residues	5
Details	binding site for residue HTO A 209

Chain	Residue
A	LYS43
A	SER95
A	ASP96
A	SO4206
C	TYR156

site_id	AD1
Number of Residues	9
Details	binding site for residue HXJ B 201

Chain	Residue
A	VAL29
A	ARG31
A	SER166
A	SER167
A	GLY168
B	THR56
B	ASN78
B	ARG79
B	HOH301

site_id	AD2
Number of Residues	8
Details	binding site for residue HXJ B 202

Chain	Residue
B	SER54
B	THR84
B	GLY85
B	TYR108
B	TYR113
B	TYR133
B	TYR137
B	SO4205

site_id	AD3
Number of Residues	8
Details	binding site for residue HXJ B 203

Chain	Residue
B	ASN111
B	TRP112
B	TYR113
B	TRP116
B	TYR137
B	PRO142
B	SO4207
B	HOH303

site_id	AD4
Number of Residues	3
Details	binding site for residue SO4 B 204

Chain	Residue
B	ARG120
B	TYR122
B	LYS123

site_id	AD5
Number of Residues	5
Details	binding site for residue SO4 B 205

Chain	Residue
B	ARG53
B	GLN130
B	TYR133
B	TYR138
B	HXJ202

site_id	AD6
Number of Residues	4
Details	binding site for residue SO4 B 206

Chain	Residue
B	ARG161
B	GLU173
B	HIS175
C	HIS63

site_id	AD7
Number of Residues	5
Details	binding site for residue SO4 B 207

Chain	Residue
B	SER114
B	TRP116
B	ARG144
B	HXJ203
B	HOH303

site_id	AD8
Number of Residues	4
Details	binding site for residue SO4 B 208

Chain	Residue
B	TRP149
B	HIS150
B	SER151
C	ARG127

site_id	AD9
Number of Residues	7
Details	binding site for residue HXJ C 201

Chain	Residue
B	ARG31
B	SER166
B	SER167
B	GLY168
C	THR56
C	ASN78
C	ARG79

site_id	AE1
Number of Residues	9
Details	binding site for residue HXJ C 202

Chain	Residue
C	TRP112
C	TYR113
C	TYR133
C	TYR137
C	SO4206
C	SER54
C	THR84
C	GLY85
C	TYR108

site_id	AE2
Number of Residues	7
Details	binding site for residue HXJ C 203

Chain	Residue
C	ASN111
C	TRP112
C	TYR113
C	TRP116
C	TYR137
C	PRO142
C	SO4208

site_id	AE3
Number of Residues	10
Details	binding site for residue HXJ C 204

Chain	Residue
C	LEU26
C	ARG31
C	TYR110
C	SER166
C	SER167
C	GLY168
D	THR56
D	ASN78
D	ARG79
D	VAL82

site_id	AE4
Number of Residues	4
Details	binding site for residue SO4 C 205

Chain	Residue
C	ARG120
C	VAL121
C	TYR122
C	LYS123

site_id	AE5
Number of Residues	5
Details	binding site for residue SO4 C 206

Chain	Residue
C	ARG53
C	GLN130
C	TYR133
C	TYR138
C	HXJ202

site_id	AE6
Number of Residues	5
Details	binding site for residue SO4 C 207

Chain	Residue
C	ARG161
C	GLU173
C	HIS175
C	HOH307
D	HIS63

site_id	AE7
Number of Residues	3
Details	binding site for residue SO4 C 208

Chain	Residue
C	SER114
C	ARG144
C	HXJ203

site_id	AE8
Number of Residues	11
Details	binding site for residue HXJ D 201

Chain	Residue
D	SER54
D	ALA83
D	THR84
D	GLY85
D	TYR108
D	TRP112
D	TYR113
D	TYR133
D	TYR137
D	SO4205
D	HOH303

site_id	AE9
Number of Residues	7
Details	binding site for residue HXJ D 202

Chain	Residue
D	ASN111
D	TRP112
D	TYR113
D	TRP116
D	TYR137
D	PRO142
D	SO4207

site_id	AF1
Number of Residues	7
Details	binding site for residue HXJ D 203

Chain	Residue
A	ASN78
A	ARG79
D	ARG31
D	TYR110
D	SER166
D	SER167
D	GLY168

site_id	AF2
Number of Residues	3
Details	binding site for residue SO4 D 204

Chain	Residue
D	ARG120
D	TYR122
D	LYS123

site_id	AF3
Number of Residues	5
Details	binding site for residue SO4 D 205

Chain	Residue
D	ARG53
D	GLN130
D	TYR133
D	TYR138
D	HXJ201

site_id	AF4
Number of Residues	4
Details	binding site for residue SO4 D 206

Chain	Residue
A	HIS63
D	ARG161
D	GLU173
D	HIS175

site_id	AF5
Number of Residues	4
Details	binding site for residue SO4 D 207

Chain	Residue
D	SER114
D	TRP116
D	ARG144
D	HXJ202

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)