10tl

Cryo-EM structure of human MOR bound with DAMGO and BMS986187

Method: ELECTRON MICROSCOPY Dmax: 89.7 Å Quality: EXCELLENT

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

Mu-type opioid receptor

Homo sapiens

UniProt P35372

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 1–388 Chain R; UniProt 1–388 Mutation:F158W TYR-DAL-GLY-MEA-ETA × 2 CLR CHOLESTEROL × 8 A1D6B 3,3,6,6-tetramethyl-9-[4-[(2-methylphenyl)methoxy]phenyl]-4,5,7,9-tetrahydro-2~{H}-xanthene-1,8-dione × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 Å R-free 0.402

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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OPRM_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain F; PDBConstruct 1–388; UniProt 1–388 Author chain R; PDBConstruct 1–388; UniProt 1–388

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 10tl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10tl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10tl
Deposition date deposition_date2026-02-08
最后修订 last_revision2026-05-27
Structure title titleCryo-EM structure of human MOR bound with DAMGO and BMS986187
Keywords keywordsanalgesics, GPCR, allosteric modulation, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.42
Radius of gyration Rg (electron density) rg_electron27.24
Forward intensity I(0) i0123878000.00
Molecular weight molecular_weight63571.0 kDa
Excluded volume excluded_volume64245 ų
Envelope volume envelope_volume110470 ų
Hydration-shell volume shell_volume33518 ų
Envelope diameter envelope_diameter93.0
Shell Rg shell_rg34.86
Envelope Rg envelope_rg27.32
Shape Rg shape_rg27.20
Total Rg total_rg27.96
Total atoms total_atoms4836
Residues n_residues568
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 dmax89.7
Rg (real space) rg_real28.31
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real1.2390e+08
I(0) uncertainty (real space) i0_real_error1.6750e+06
Rg (reciprocal space) rg_reciprocal28.35
I(0) (reciprocal space) i0_reciprocal123900000.0000
Solution quality estimate total_estimate0.9074
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.0
Skewness Skewness skewness0.175
Kurtosis Kurtosis kurtosis-0.575
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18250000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.972

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)