Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4LSI

Ion selectivity of OmpF porin soaked in 0.3M KBr

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001530	molecular_function	lipopolysaccharide binding
A	0005216	molecular_function	monoatomic ion channel activity
A	0005515	molecular_function	protein binding
A	0006811	biological_process	monoatomic ion transport
A	0008289	molecular_function	lipid binding
A	0009279	cellular_component	cell outer membrane
A	0015031	biological_process	protein transport
A	0015288	molecular_function	porin activity
A	0016020	cellular_component	membrane
A	0034220	biological_process	monoatomic ion transmembrane transport
A	0034702	cellular_component	monoatomic ion channel complex
A	0042802	molecular_function	identical protein binding
A	0042912	molecular_function	colicin transmembrane transporter activity
A	0043213	biological_process	bacteriocin transport
A	0046930	cellular_component	pore complex
A	0070207	biological_process	protein homotrimerization
A	0097718	molecular_function	disordered domain specific binding
B	0001530	molecular_function	lipopolysaccharide binding
B	0005216	molecular_function	monoatomic ion channel activity
B	0005515	molecular_function	protein binding
B	0006811	biological_process	monoatomic ion transport
B	0008289	molecular_function	lipid binding
B	0009279	cellular_component	cell outer membrane
B	0015031	biological_process	protein transport
B	0015288	molecular_function	porin activity
B	0016020	cellular_component	membrane
B	0034220	biological_process	monoatomic ion transmembrane transport
B	0034702	cellular_component	monoatomic ion channel complex
B	0042802	molecular_function	identical protein binding
B	0042912	molecular_function	colicin transmembrane transporter activity
B	0043213	biological_process	bacteriocin transport
B	0046930	cellular_component	pore complex
B	0070207	biological_process	protein homotrimerization
B	0097718	molecular_function	disordered domain specific binding
C	0001530	molecular_function	lipopolysaccharide binding
C	0005216	molecular_function	monoatomic ion channel activity
C	0005515	molecular_function	protein binding
C	0006811	biological_process	monoatomic ion transport
C	0008289	molecular_function	lipid binding
C	0009279	cellular_component	cell outer membrane
C	0015031	biological_process	protein transport
C	0015288	molecular_function	porin activity
C	0016020	cellular_component	membrane
C	0034220	biological_process	monoatomic ion transmembrane transport
C	0034702	cellular_component	monoatomic ion channel complex
C	0042802	molecular_function	identical protein binding
C	0042912	molecular_function	colicin transmembrane transporter activity
C	0043213	biological_process	bacteriocin transport
C	0046930	cellular_component	pore complex
C	0070207	biological_process	protein homotrimerization
C	0097718	molecular_function	disordered domain specific binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 401

Chain	Residue
A	ASP121
A	HOH652

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 402

Chain	Residue
A	ASP113
A	MET114
A	ARG270
A	HOH666

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE C8E A 403

Chain	Residue
A	LEU227
A	ALA228
A	VAL260

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 404

Chain	Residue
A	ARG82
A	ASP113
A	ARG132

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL A 405

Chain	Residue
A	VAL11

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 406

Chain	Residue
A	GLU201
A	GLN203
A	GLY206

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 407

Chain	Residue
A	ASN316
A	ILE318
A	SER328
A	HOH557
A	HOH595

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BR A 408

Chain	Residue
A	SER125
A	ARG167

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE BR A 409

Chain	Residue
A	HOH514

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BR A 410

Chain	Residue
A	TYR102
A	GLY103
A	VAL104
A	TYR106
A	PHE129
A	VAL130
A	GLY131

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BR A 411

Chain	Residue
A	MET114
A	LEU115
A	PRO116
A	GLN262
A	SER272

site_id	BC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PEG A 412

Chain	Residue
A	GLN66
A	GLY67
A	ASN68
A	ASN69
A	SER70
A	ALA75
A	ASN79
C	LYS80
C	THR81
C	ARG100

site_id	BC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PEG B 401

Chain	Residue
A	LYS80
A	THR81
A	ARG100
B	GLN66
B	ASN69
B	SER70
B	GLU71
B	ALA75
B	ASN79
B	HOH503

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG B 402

Chain	Residue
B	HOH639
B	HOH646

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG B 403

Chain	Residue
B	ARG140
B	ASN141
B	SER142
B	PHE153
B	SER177
B	SER179
B	HOH656

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE C8E B 404

Chain	Residue
B	PHE267
B	TYR301
C	TYR313

site_id	BC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE C8E B 405

Chain	Residue
B	LEU259
B	ILE273

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 406

Chain	Residue
B	ARG82
B	ASP113
B	ARG132

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 407

Chain	Residue
B	GLU201
B	GLN203
B	GLY206
B	HOH601
B	HOH673

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 408

Chain	Residue
B	ASN316
B	ILE318
B	SER328
B	HOH600
C	HOH663

site_id	CC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BR B 410

Chain	Residue
B	SER125
B	ARG167

site_id	CC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE BR B 411

Chain	Residue
B	ILE51

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE C8E C 401

Chain	Residue
C	TYR98
C	GLY159
C	GLY173
C	HOH586

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 402

Chain	Residue
C	ASN207
C	ASN236
C	ASN252
C	HOH588
C	HOH593

site_id	CC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 403

Chain	Residue
B	HOH532
C	ASN69
C	ASP74
C	HOH636

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 404

Chain	Residue
C	GLU201
C	GLN203
C	GLY206
C	HOH606
C	HOH676

site_id	CC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 405

Chain	Residue
C	ASN316
C	ILE318
C	SER328

site_id	DC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PEG C 406

Chain	Residue
C	ASP126
C	ASP127
C	PHE128
C	GLY134
C	ARG163
C	ARG167
C	ARG168
C	SER169
C	ASN170
C	GLN200

site_id	DC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PEG C 407

Chain	Residue
B	LYS80
B	THR81
C	GLN66
C	ASN69
C	SER70
C	GLU71
C	ALA75
C	ASN79
C	HOH504

site_id	DC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 409

Chain	Residue
C	ASP113
C	ARG132
C	HOH640

site_id	DC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BR C 410

Chain	Residue
C	LYS16
C	HOH506
C	HOH600

site_id	DC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BR C 411

Chain	Residue
C	SER125
C	ARG167

Functional Information from PROSITE/UniProt

site_id	PS00576
Number of Residues	17
Details	GRAM_NEG_PORIN General diffusion Gram-negative porins signature. FevGatYyFnKnmSTYV

Chain	Residue	Details
A	PHE295-VAL311

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	42
Details	Topological domain: {"description":"Periplasmic"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	495
Details	Transmembrane: {"description":"Beta stranded"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	378
Details	Topological domain: {"description":"Extracellular"}

Chain

Residue

Details

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