Structure of PDB 5enq Chain C

Receptor sequence
>5enqC (length=578) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
APPAVTISASYPGADAKTVQDTVTQVIEQNMNGIDNLMYMSSNSDSTGTV
QITLTFESGTDADIAQVQVQNKLQLAMPLLPQEVQQQGVSVEKSSSSFLM
VVGVINTDGTMTQEDISDYVAANMKDAISRTSGVGDVQLFGSQYAMRIWM
NPNELNKFQLTPVDVITAIKAQNAQVAAGQLGGTPPVKGQQLNASIIAQT
RLTSTEEFGKILLKVNQDGSRVLLRDVAKIELGGENYDIIAEFNGQPASG
LGIKLATGANALDTAAAIRAELAKMEPFFPSGLKIVYPYDTGVFMTMVQL
PAGATQERTQKVLNEVTHYYLTKEKNNVESVFAVNGFGFAGRGQNTGIAF
VSLKDWADRPGEENKVEAITMRATRAFSQIKDAMVFAFNLATGFDFELID
QAGLGHEKLTQARNQLLAEAAKHPDMLTSVRPNGLEDTPQFKIDIDQEKA
QALGVSINDINTTLGAAWGGSYVNDFIDRGRVKKVYVMSEAKYRMLPDDI
GDWYVRAADGQMVPFSAFSSSRWEYGSPRLERYNGLPSMEILGQAAPGKS
TGEAMELMEQLASKLPTGVGYDWTGMSY
3D structure
PDB5enq Molecular basis for inhibition of AcrB multidrug efflux pump by novel and powerful pyranopyridine derivatives.
ChainC
Resolution1.8 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 5QE C F178 I277 A279 Y327 F610 F615 F628 F140 I239 A241 Y289 F332 F337 F350
Gene Ontology
Molecular Function
GO:0022857 transmembrane transporter activity
Biological Process
GO:0055085 transmembrane transport
Cellular Component
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5enq, PDBe:5enq, PDBj:5enq
PDBsum5enq
PubMed26976576
UniProtP31224|ACRB_ECOLI Multidrug efflux pump subunit AcrB (Gene Name=acrB)

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