Structure of PDB 5nuo Chain C

Receptor sequence
>5nuoC (length=340) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
AEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQ
INSDLTGYGQWEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGR
NYGVVYDALGYTDMLPEFGGDTAYSDDFFVGRVGGVATYRNSNFFGLVDG
LNFAVQYLGKNERDTARRSNGDGVGGSISYEYEGFGIVGAYGAADRTNLQ
EAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPITNKFTNTSGF
ANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVGAT
YYFNKNMSTYVDYIINQIDSDNKLGVGSDDTVAVGIVYQF
3D structure
PDB5nuo Structural basis for maintenance of bacterial outer membrane lipid asymmetry.
ChainC
Resolution3.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 C8E C Y263 F265 Y263 F265
BS02 C8E C V297 G298 V297 G298
BS03 C8E C Y98 Y157 Y98 Y157
Gene Ontology
Molecular Function
GO:0001530 lipopolysaccharide binding
GO:0005216 monoatomic ion channel activity
GO:0005515 protein binding
GO:0008289 lipid binding
GO:0015288 porin activity
GO:0042802 identical protein binding
GO:0042912 colicin transmembrane transporter activity
GO:0097718 disordered domain specific binding
Biological Process
GO:0006811 monoatomic ion transport
GO:0015031 protein transport
GO:0034220 monoatomic ion transmembrane transport
GO:0043213 bacteriocin transport
GO:0070207 protein homotrimerization
Cellular Component
GO:0009279 cell outer membrane
GO:0016020 membrane
GO:0034702 monoatomic ion channel complex
GO:0046930 pore complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5nuo, PDBe:5nuo, PDBj:5nuo
PDBsum5nuo
PubMed29038444
UniProtP02931|OMPF_ECOLI Outer membrane porin F (Gene Name=ompF)

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