Structure of PDB 1gfo Chain A

Receptor sequence
>1gfoA (length=340) Species: 562 (Escherichia coli) [Search protein sequence]
AEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQ
INSDLTGYGQWEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGR
NYGVVYDALGYTDMLPEFGGDTAYSDDFFVGPVGGVATYRNSNFFGLVDG
LNFAVQYLGKNERDTARRSNGDGVGGSISYEYEGFGIVGAYGAADRTNLQ
EAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPITNKFTNTSGF
ANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVGAT
YYFNKNMSTYVDYIINQIDSDNKLGVGSDDTVAVGIVYQF
3D structure
PDB1gfo Structural and functional characterization of OmpF porin mutants selected for larger pore size. I. Crystallographic analysis.
ChainA
Resolution3.3 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 A Y313 V332 Y313 V332
BS02 C8E A I178 Y191 I178 Y191
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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Biological Process
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Cellular Component
External links
PDB RCSB:1gfo, PDBe:1gfo, PDBj:1gfo
PDBsum1gfo
PubMed8702816
UniProtP02931|OMPF_ECOLI Outer membrane porin F (Gene Name=ompF)

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