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3POU

Crystal structure of E.coli OmpF porin in lipidic cubic phase: space group H32, large unit cell

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
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OLC A 341
ChainResidue
APHE23
ATYR98
ATYR157
AGLY159
AASP172
AVAL311
AVAL334
AHOH369

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE OLC A 342
ChainResidue
ATYR180

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OLC A 343
ChainResidue
ASER177
AILE178
AALA190
ATRP214

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE OLC A 344
ChainResidue
ALEU218
AILE273

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 Residues170
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

site_idSWS_FT_FI2
Number of Residues14
DetailsTOPO_DOM: Periplasmic
ChainResidueDetails
AASN52-SER53
AASP92-VAL93
ASER142-ASP149
AASP266-PHE267
AASN304-LYS305
AASP7
AGLU183
AASN223

site_idSWS_FT_FI3
Number of Residues126
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
ASER24-MET38
AGLY67-ARG82
AASN101-GLY134
ALYS160-GLY171
AARG196-LYS210
AASN236-ASN252
AASP282-LEU291
AASN316-ASP330

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PDB entries from 2024-05-15

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