Structure of PDB 3eyw Chain A

Receptor sequence
>3eywA (length=337) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MRVIIAGFGRFGQITGRLLLSSGVKMVVLDHDPDHIETLRKFGMKVFYGD
ATRMDLLESAGAAKAEVLINAIDDPQTNLQLTEMVKEHFPHLQIIARARD
VDHYIRLRQAGVEKPERETFEGALKTGRLALESLGLGPYEARERADVFRR
FNIQMVEEMAMVEMILIIYAHPYPHHSHANKRMLEQARTLEGVEIRSLYQ
LYPDFNIDIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVFSHGWA
YGHGGTALHGKHLLWAVTTGGGESHFEIGAHPGFDVLSQPLQATAIYCGL
NWLPPFAMHCTFICDDETLEGQARHYKQRLLEWQEAH
3D structure
PDB3eyw KTN (RCK) Domains Regulate K(+) Channels and Transporters by Controlling the Dimer-Hinge Conformation.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G1107 F1113 H1118
Catalytic site (residue number reindexed from 1) G270 F276 H281
Enzyme Commision number ?
1.6.5.2: NAD(P)H dehydrogenase (quinone).
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003955 NAD(P)H dehydrogenase (quinone) activity
GO:0005515 protein binding
GO:0008753 NADPH dehydrogenase (quinone) activity
GO:0009055 electron transfer activity
GO:0010181 FMN binding
GO:0015079 potassium ion transmembrane transporter activity
GO:0016491 oxidoreductase activity
GO:0042803 protein homodimerization activity
GO:0050136 NADH:ubiquinone reductase (non-electrogenic) activity
Biological Process
GO:0006813 potassium ion transport
GO:0032414 positive regulation of ion transmembrane transporter activity
GO:0051453 regulation of intracellular pH
GO:0051454 intracellular pH elevation
GO:1901381 positive regulation of potassium ion transmembrane transport
Cellular Component
GO:0005886 plasma membrane
GO:1903103 potassium:proton antiporter complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3eyw, PDBe:3eyw, PDBj:3eyw
PDBsum3eyw
PubMed19523906
UniProtP03819|KEFC_ECOLI Glutathione-regulated potassium-efflux system protein KefC (Gene Name=kefC);
P0A754

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