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- PDB-9i7v: EAAT1 thermostabilized mutant in Complex with Rubidium, and the a... -

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Basic information

Entry
Database: PDB / ID: 9i7v
TitleEAAT1 thermostabilized mutant in Complex with Rubidium, and the allosteric inhibitor UCPH101 in DDS/CHS
ComponentsEAAT1 thermostabilized mutant
KeywordsMEMBRANE PROTEIN / TRANSPORT PROTEIN / Glutamate transport / Salipro / L-aspartate
Function / homologyChem-6Z6 / 1,2-DIPALMITOYL-SN-GLYCERO-3-PHOSPHATE / RUBIDIUM ION
Function and homology information
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.84 Å
AuthorsHorn, G. / Fu, L. / Madej, M.G. / Ziegler, C.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research Foundation (DFG)2518 Germany
CitationJournal: To Be Published
Title: CryoEM Structure of EAAT1 thermostabilized mutant in Complex with L-Asp, Metal Ions, and the allosteric inhibitor UCPH101 in Salipro and DDS/CHS
Authors: Horn, G. / Fu, L. / Madej, M.G. / Ziegler, C.
History
DepositionFeb 2, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 18, 2026Provider: repository / Type: Initial release
Revision 1.0Feb 18, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Feb 18, 2026Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Feb 18, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Feb 18, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Feb 18, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Feb 18, 2026Data content type: Mask / Part number: 1 / Data content type: Mask / Provider: repository / Type: Initial release
Revision 1.0Feb 18, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: EAAT1 thermostabilized mutant
B: EAAT1 thermostabilized mutant
C: EAAT1 thermostabilized mutant
hetero molecules


Theoretical massNumber of molelcules
Total (without water)173,00512
Polymers169,5373
Non-polymers3,4679
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.5, -0.866025), (0.866025, -0.5), (1)238.97991, 64.03449
3given(-0.5, 0.866025), (-0.866025, -0.5), (1)64.03449, 238.97991

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Components

#1: Protein EAAT1 thermostabilized mutant


Mass: 56512.379 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human)
#2: Chemical ChemComp-PX6 / 1,2-DIPALMITOYL-SN-GLYCERO-3-PHOSPHATE


Mass: 647.883 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C35H68O8P
#3: Chemical ChemComp-6Z6 / 2-Amino-5,6,7,8-tetrahydro-4-(4-methoxyphenyl)-7-(naphthalen-1-yl)-5-oxo-4H-chromene-3-carbonitrile


Mass: 422.475 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C27H22N2O3 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-RB / RUBIDIUM ION


Mass: 85.468 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Rb
Has ligand of interestY
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Excitatory amino acid transporter 1, SLC1A3 / Type: COMPLEX / Details: EAAT1 thermostabilized mutant / Entity ID: #1 / Source: RECOMBINANT
Molecular weightValue: 0.169 MDa / Experimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 7.4
Buffer component
IDConc.NameBuffer-ID
125 mMHEPES/TRIS1
2100 mMNaCl1
3100 mMRbCl1
41 mMTCEP1
50.1 mMUCHP1011
60.05 %DDS1
70.01 %CHS1
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K

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Electron microscopy imaging

MicroscopyModel: JEOL CRYO ARM 200
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 1600 nm / Nominal defocus min: 600 nm / C2 aperture diameter: 70 µm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: JEOL CRYOSPECPORTER
Image recordingElectron dose: 66 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 4978
EM imaging opticsEnergyfilter name: In-column Omega Filter / Energyfilter slit width: 20 eV

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Processing

EM software
IDNameVersionCategory
1RELION4particle selection
2SerialEMimage acquisition
4CTFFIND4.4.11CTF correction
7UCSF Chimeramodel fitting
9RELION4initial Euler assignment
10cryoSPARCV4final Euler assignment
11RELION4classification
12cryoSPARCV43D reconstruction
13REFMAC5model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 1000401
SymmetryPoint symmetry: C3 (3 fold cyclic)
3D reconstructionResolution: 3.84 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 63000 / Symmetry type: POINT
Atomic model buildingProtocol: FLEXIBLE FIT / Space: REAL
Atomic model buildingPDB-ID: 9I7M

9i7m


Accession code: 9I7M / Source name: PDB / Type: experimental model
RefinementResolution: 3.84→121.52 Å / Cor.coef. Fo:Fc: 0.582 / SU B: 52.649 / SU ML: 0.704 / ESU R: 0.601
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflection
Rwork0.47126 --
obs0.47126 41443 100 %
Solvent computationSolvent model: PARAMETERS FOR MASK CACLULATION
Displacement parametersBiso mean: 85.589 Å2
Refinement stepCycle: 1 / Total: 3175
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
ELECTRON MICROSCOPYr_bond_refined_d0.0060.0123228
ELECTRON MICROSCOPYr_bond_other_d00.0163304
ELECTRON MICROSCOPYr_angle_refined_deg1.4111.7854389
ELECTRON MICROSCOPYr_angle_other_deg0.5051.6847546
ELECTRON MICROSCOPYr_dihedral_angle_1_deg4.2045415
ELECTRON MICROSCOPYr_dihedral_angle_2_deg17.991521
ELECTRON MICROSCOPYr_dihedral_angle_3_deg15.28610521
ELECTRON MICROSCOPYr_dihedral_angle_4_deg
ELECTRON MICROSCOPYr_chiral_restr0.0640.2555
ELECTRON MICROSCOPYr_gen_planes_refined0.0050.023609
ELECTRON MICROSCOPYr_gen_planes_other0.0010.02685
ELECTRON MICROSCOPYr_nbd_refined
ELECTRON MICROSCOPYr_nbd_other
ELECTRON MICROSCOPYr_nbtor_refined
ELECTRON MICROSCOPYr_nbtor_other
ELECTRON MICROSCOPYr_xyhbond_nbd_refined
ELECTRON MICROSCOPYr_xyhbond_nbd_other
ELECTRON MICROSCOPYr_metal_ion_refined
ELECTRON MICROSCOPYr_metal_ion_other
ELECTRON MICROSCOPYr_symmetry_vdw_refined
ELECTRON MICROSCOPYr_symmetry_vdw_other
ELECTRON MICROSCOPYr_symmetry_hbond_refined
ELECTRON MICROSCOPYr_symmetry_hbond_other
ELECTRON MICROSCOPYr_symmetry_metal_ion_refined
ELECTRON MICROSCOPYr_symmetry_metal_ion_other
ELECTRON MICROSCOPYr_mcbond_it6.2268.2681670
ELECTRON MICROSCOPYr_mcbond_other6.2148.2711669
ELECTRON MICROSCOPYr_mcangle_it10.77114.8532081
ELECTRON MICROSCOPYr_mcangle_other10.77214.8662082
ELECTRON MICROSCOPYr_scbond_it9.1199.391558
ELECTRON MICROSCOPYr_scbond_other9.1199.3951559
ELECTRON MICROSCOPYr_scangle_it
ELECTRON MICROSCOPYr_scangle_other16.19116.9332309
ELECTRON MICROSCOPYr_long_range_B_refined24.39296.9813344
ELECTRON MICROSCOPYr_long_range_B_other24.39196.9913345
ELECTRON MICROSCOPYr_rigid_bond_restr
ELECTRON MICROSCOPYr_sphericity_free
ELECTRON MICROSCOPYr_sphericity_bonded
LS refinement shellResolution: 3.84→3.94 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0 0 -
Rwork1.781 3052 -
obs--100 %

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