Structure of PDB 3eyw Chain A Binding Site BS02

Receptor Information
>3eyw Chain A (length=337) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRVIIAGFGRFGQITGRLLLSSGVKMVVLDHDPDHIETLRKFGMKVFYGD
ATRMDLLESAGAAKAEVLINAIDDPQTNLQLTEMVKEHFPHLQIIARARD
VDHYIRLRQAGVEKPERETFEGALKTGRLALESLGLGPYEARERADVFRR
FNIQMVEEMAMVEMILIIYAHPYPHHSHANKRMLEQARTLEGVEIRSLYQ
LYPDFNIDIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVFSHGWA
YGHGGTALHGKHLLWAVTTGGGESHFEIGAHPGFDVLSQPLQATAIYCGL
NWLPPFAMHCTFICDDETLEGQARHYKQRLLEWQEAH
Ligand information
Ligand IDNAD
InChIInChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBAWFJGJZGIEFAR-NNYOXOHSSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
FormulaC21 H27 N7 O14 P2
NameNICOTINAMIDE-ADENINE-DINUCLEOTIDE
ChEMBLCHEMBL1234613
DrugBankDB14128
ZINC
PDB chain3eyw Chain A Residue 2401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3eyw KTN (RCK) Domains Regulate K(+) Channels and Transporters by Controlling the Dimer-Hinge Conformation.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		G408 R409 F410 D429 H430 D431 H434 D449 A450 I471 D472 R496
Binding residue
(residue number reindexed from 1)		G9 R10 F11 D30 H31 D32 H35 D50 A51 I72 D73 R97
Annotation score4
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).
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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