Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4LSE

Ion selectivity of OmpF porin soaked in 0.2M NaBr

Functional Information from GO Data
ChainGOidnamespacecontents
A0001530molecular_functionlipopolysaccharide binding
A0005216molecular_functionmonoatomic ion channel activity
A0005515molecular_functionprotein binding
A0006811biological_processmonoatomic ion transport
A0008289molecular_functionlipid binding
A0009279cellular_componentcell outer membrane
A0015031biological_processprotein transport
A0015288molecular_functionporin activity
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0042802molecular_functionidentical protein binding
A0042912molecular_functioncolicin transmembrane transporter activity
A0043213biological_processbacteriocin transport
A0046930cellular_componentpore complex
A0070207biological_processprotein homotrimerization
A0097718molecular_functiondisordered domain specific binding
B0001530molecular_functionlipopolysaccharide binding
B0005216molecular_functionmonoatomic ion channel activity
B0005515molecular_functionprotein binding
B0006811biological_processmonoatomic ion transport
B0008289molecular_functionlipid binding
B0009279cellular_componentcell outer membrane
B0015031biological_processprotein transport
B0015288molecular_functionporin activity
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
B0034702cellular_componentmonoatomic ion channel complex
B0042802molecular_functionidentical protein binding
B0042912molecular_functioncolicin transmembrane transporter activity
B0043213biological_processbacteriocin transport
B0046930cellular_componentpore complex
B0070207biological_processprotein homotrimerization
B0097718molecular_functiondisordered domain specific binding
C0001530molecular_functionlipopolysaccharide binding
C0005216molecular_functionmonoatomic ion channel activity
C0005515molecular_functionprotein binding
C0006811biological_processmonoatomic ion transport
C0008289molecular_functionlipid binding
C0009279cellular_componentcell outer membrane
C0015031biological_processprotein transport
C0015288molecular_functionporin activity
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
C0034702cellular_componentmonoatomic ion channel complex
C0042802molecular_functionidentical protein binding
C0042912molecular_functioncolicin transmembrane transporter activity
C0043213biological_processbacteriocin transport
C0046930cellular_componentpore complex
C0070207biological_processprotein homotrimerization
C0097718molecular_functiondisordered domain specific binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR A 401
ChainResidue
ALYS16

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR A 402
ChainResidue
AGLN66
AASN68
AHOH582
AHOH607

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR A 403
ChainResidue
ASER125
AARG167

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR A 404
ChainResidue
ATYR40
AMET38
ATHR39

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 405
ChainResidue
AHOH696

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 406
ChainResidue
AASN207
AASN236
AASN252

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG A 407
ChainResidue
ATYR32
AHOH696

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE C8E A 408
ChainResidue
AALA228
AALA261

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BR B 401
ChainResidue
AASP126
AARG168
BSER70
BGLU71
BGLY72

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR B 402
ChainResidue
BLYS16
BHOH516

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG B 403
ChainResidue
BPEG404

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG B 404
ChainResidue
BTYR32
BASP121
BMG403

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE C8E B 405
ChainResidue
BVAL174

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR B 406
ChainResidue
BPHE45
CLYS16
CALA17
CARG42

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 407
ChainResidue
BASN207
BASN236
BASN252
BHOH572
BHOH609
BHOH622

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 401
ChainResidue
CASN207
CASN236
CASN252
CHOH617
CHOH625

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 403
ChainResidue
CARG168
CASN170
CHOH703
CHOH704

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG C 404
ChainResidue
CALA166
CARG167
CSER248
CGLY249

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG C 405
ChainResidue
CTYR22
CGLU117
CHOH706

Functional Information from PROSITE/UniProt
site_idPS00576
Number of Residues17
DetailsGRAM_NEG_PORIN General diffusion Gram-negative porins signature. FevGatYyFnKnmSTYV
ChainResidueDetails
APHE295-VAL311

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues510
DetailsTRANSMEM: Beta stranded
ChainResidueDetails
AALA1-LYS6
AGLY8-PHE23
ATHR39-ILE51
AASP54-GLN66
ALEU83-ALA91
AGLY94-ARG100
AGLY135-ASN141
AGLY150-GLY159
AASP172-TYR182
AGLY184-ASP195
AALA211-ALA222
AASN224-ARG235
ALYS253-PHE265
AGLY268-LYS281
AVAL292-PHE303
AASN306-ILE315
ATHR331-PHE340
BALA1-LYS6
BGLY8-PHE23
BTHR39-ILE51
BASP54-GLN66
BLEU83-ALA91
BGLY94-ARG100
BGLY135-ASN141
BGLY150-GLY159
BASP172-TYR182
BGLY184-ASP195
BALA211-ALA222
BASN224-ARG235
BLYS253-PHE265
BGLY268-LYS281
BVAL292-PHE303
BASN306-ILE315
BTHR331-PHE340
CALA1-LYS6
CGLY8-PHE23
CTHR39-ILE51
CASP54-GLN66
CLEU83-ALA91
CGLY94-ARG100
CGLY135-ASN141
CGLY150-GLY159
CASP172-TYR182
CGLY184-ASP195
CALA211-ALA222
CASN224-ARG235
CLYS253-PHE265
CGLY268-LYS281
CVAL292-PHE303
CASN306-ILE315
CTHR331-PHE340

site_idSWS_FT_FI2
Number of Residues42
DetailsTOPO_DOM: Periplasmic
ChainResidueDetails
AASN52-SER53
AASP92-VAL93
ASER142-ASP149
AASP266-PHE267
AASN304-LYS305
BASN52-SER53
BASP92-VAL93
BSER142-ASP149
BASP266-PHE267
BASN304-LYS305
CASN52-SER53
CASP92-VAL93
CSER142-ASP149
CASP266-PHE267
CASN304-LYS305
AASP7
AGLU183
AASN223
BASP7
BGLU183
BASN223
CASP7
CGLU183
CASN223

site_idSWS_FT_FI3
Number of Residues378
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
ASER24-MET38
AGLY67-ARG82
AASN101-GLY134
ALYS160-GLY171
AARG196-LYS210
AASN236-ASN252
AASP282-LEU291
AASN316-ASP330
BSER24-MET38
BGLY67-ARG82
BASN101-GLY134
BLYS160-GLY171
BARG196-LYS210
BASN236-ASN252
BASP282-LEU291
BASN316-ASP330
CSER24-MET38
CGLY67-ARG82
CASN101-GLY134
CLYS160-GLY171
CARG196-LYS210
CASN236-ASN252
CASP282-LEU291
CASN316-ASP330

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon