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- PDB-6w83: K2P2.1 (TREK-1), 100 mM K+ -

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Basic information

Entry
Database: PDB / ID: 6w83
TitleK2P2.1 (TREK-1), 100 mM K+
ComponentsPotassium channel subfamily K member 2
KeywordsMETAL TRANSPORT / ion channel / K2P / TREK1 / TREK-1
Function / homology
Function and homology information


TWIK related potassium channel (TREK) / Phase 4 - resting membrane potential / positive regulation of cellular response to hypoxia / cardiac ventricle development / negative regulation of cardiac muscle cell proliferation / stabilization of membrane potential / potassium ion leak channel activity / astrocyte projection / potassium channel inhibitor activity / negative regulation of DNA biosynthetic process ...TWIK related potassium channel (TREK) / Phase 4 - resting membrane potential / positive regulation of cellular response to hypoxia / cardiac ventricle development / negative regulation of cardiac muscle cell proliferation / stabilization of membrane potential / potassium ion leak channel activity / astrocyte projection / potassium channel inhibitor activity / negative regulation of DNA biosynthetic process / outward rectifier potassium channel activity / cochlea development / voltage-gated potassium channel activity / calyx of Held / response to axon injury / response to mechanical stimulus / axon terminus / potassium ion transmembrane transport / voltage-gated potassium channel complex / regulation of membrane potential / potassium ion transport / memory / cellular response to hypoxia / G protein-coupled receptor signaling pathway / apical plasma membrane / axon / neuronal cell body / cell surface / endoplasmic reticulum / plasma membrane
Similarity search - Function
Two pore domain potassium channel, TREK / Two pore domain potassium channel / Potassium channel domain / Ion channel
Similarity search - Domain/homology
: / DECANE / DODECANE / : / N-OCTANE / HEXADECANE / Potassium channel subfamily K member 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.901 Å
AuthorsLolicato, M. / Minor, D.L.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Mental Health (NIH/NIMH)NIH-R01-MH093603 United States
CitationJournal: Sci Adv / Year: 2020
Title: K 2P channel C-type gating involves asymmetric selectivity filter order-disorder transitions.
Authors: Lolicato, M. / Natale, A.M. / Abderemane-Ali, F. / Crottes, D. / Capponi, S. / Duman, R. / Wagner, A. / Rosenberg, J.M. / Grabe, M. / Minor Jr., D.L.
History
DepositionMar 20, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 27, 2021Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Potassium channel subfamily K member 2
B: Potassium channel subfamily K member 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,23218
Polymers68,6082
Non-polymers1,62416
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12390 Å2
ΔGint-96 kcal/mol
Surface area31960 Å2
MethodPISA
Unit cell
Length a, b, c (Å)70.222, 121.164, 129.426
Angle α, β, γ (deg.)90, 90, 90
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Potassium channel subfamily K member 2 / Outward rectifying potassium channel protein TREK-1 / TREK-1 K(+) channel subunit / Two pore ...Outward rectifying potassium channel protein TREK-1 / TREK-1 K(+) channel subunit / Two pore potassium channel TPKC1


Mass: 34303.938 Da / Num. of mol.: 2
Mutation: K84R, Q85E, T86K, I88L, A89R, Q90A, A92P, N95S, S96D, T97Q, N119A, S300A, E306A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Kcnk2 / Production host: Komagataella pastoris (fungus) / References: UniProt: P97438

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Non-polymers , 6 types, 16 molecules

#2: Chemical ChemComp-CD / CADMIUM ION


Mass: 112.411 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cd
#3: Chemical ChemComp-D12 / DODECANE


Mass: 170.335 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C12H26
#4: Chemical ChemComp-OCT / N-OCTANE


Mass: 114.229 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C8H18
#5: Chemical
ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: K
#6: Chemical ChemComp-R16 / HEXADECANE


Mass: 226.441 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C16H34
#7: Chemical ChemComp-D10 / DECANE


Mass: 142.282 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H22

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Details

Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 4.01 Å3/Da / Density % sol: 69.35 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 22-25% PEG400, 100mM HEPES pH=8.0, 1mM CdCl2, 200mM KCl

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.0332 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 1, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
ReflectionResolution: 3.9→47.59 Å / Num. obs: 10566 / % possible obs: 99.9 % / Redundancy: 11.7 % / Rmerge(I) obs: 0.259 / Net I/σ(I): 6.2
Reflection shellResolution: 3.9→4.36 Å / Num. unique obs: 2932 / CC1/2: 0.113

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Processing

Software
NameVersionClassification
BUSTER2.10.3 (6-FEB-2020)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6cq6

6cq6


Resolution: 3.901→14.95 Å / Cor.coef. Fo:Fc: 0.93 / Cor.coef. Fo:Fc free: 0.883 / Cross valid method: THROUGHOUT / SU Rfree Blow DPI: 0.766
RfactorNum. reflection% reflectionSelection details
Rfree0.3116 465 -RANDOM
Rwork0.2422 ---
obs0.2458 10310 100 %-
Displacement parametersBiso mean: 217.38 Å2
Baniso -1Baniso -2Baniso -3
1--16.7013 Å20 Å20 Å2
2--20.2021 Å20 Å2
3----3.5008 Å2
Refine analyzeLuzzati coordinate error obs: 0.82 Å
Refinement stepCycle: LAST / Resolution: 3.901→14.95 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4283 0 83 0 4366
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.0064456HARMONIC2
X-RAY DIFFRACTIONt_angle_deg0.976029HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d1493SINUSOIDAL2
X-RAY DIFFRACTIONt_gen_planes711HARMONIC5
X-RAY DIFFRACTIONt_it4389HARMONIC10
X-RAY DIFFRACTIONt_chiral_improper_torsion606SEMIHARMONIC5
X-RAY DIFFRACTIONt_ideal_dist_contact4220SEMIHARMONIC4
X-RAY DIFFRACTIONt_omega_torsion6.01
X-RAY DIFFRACTIONt_other_torsion12.39
LS refinement shellResolution: 3.901→3.96 Å
RfactorNum. reflection% reflection
Rfree0.2321 19 -
Rwork0.2768 --
obs--99.33 %
Refinement TLS params.

Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.0327-0.31160.29460.0798-0.2340.72790.00310.0435-0.0110.04350.024-0.0504-0.011-0.0504-0.027-0.00530.0053-0.00070.0010.02-0.0105-1.8079-20.9213-21.208
20.1185-0.52280.61511.10441.02561.19330.00230.01460.02830.01460.00090.01230.02830.0123-0.0031-0.0023-0.0085-0.0009-0.02240.0057-0.00184.7192-27.3944-33.6571
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1{ A|* }
2X-RAY DIFFRACTION2{ B|* }

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