8y6h

P-glycoprotein in complex with UIC2 Fab and triple elacridar molecules in LMNG detergent

Method: ELECTRON MICROSCOPY Dmax: 152.3 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

ATP-dependent translocase ABCB1,mNeonGreen

Homo sapiens

UniProt A0A1S4NYF2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 27–260 Not recorded UIC2 Fab light chain × 1 UIC2 Fab heavy chain × 1 R0Z elacridar × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.49 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A1S4NYF2_BRALA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1293–1526; UniProt 27–260

ATP-dependent translocase ABCB1,mNeonGreen

Homo sapiens

UniProt P08183

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–1280 Not recorded UIC2 Fab light chain × 1 UIC2 Fab heavy chain × 1 R0Z elacridar × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.49 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

21 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MDR1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1280; UniProt 1–1280

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8y6h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8y6h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8y6h
Deposition date deposition_date2024-02-02
Structure title titleP-glycoprotein in complex with UIC2 Fab and triple elacridar molecules in LMNG detergent
Keywords keywordsABC transporter, elacridar, P-glycoprotein, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier41.59
Radius of gyration Rg (electron density) rg_electron41.65
Forward intensity I(0) i0144383000.00
Molecular weight molecular_weight104160.0 kDa
Excluded volume excluded_volume132820 ų
Envelope volume envelope_volume175150 ų
Hydration-shell volume shell_volume38932 ų
Envelope diameter envelope_diameter158.5
Shell Rg shell_rg40.94
Envelope Rg envelope_rg43.02
Shape Rg shape_rg41.61
Total Rg total_rg41.75
Total atoms total_atoms7370
Residues n_residues976
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax152.3
Rg (real space) rg_real42.20
Rg uncertainty (real space) rg_real_error2.26
I(0) (real space) i0_real1.4440e+08
I(0) uncertainty (real space) i0_real_error2.9820e+06
Rg (reciprocal space) rg_reciprocal41.60
I(0) (reciprocal space) i0_reciprocal144300000.0000
Solution quality estimate total_estimate0.7445
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.1
Skewness Skewness skewness0.652
Kurtosis Kurtosis kurtosis-0.261
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10970000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.488; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.507; Smooth: 0.703

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)