9ejl

Lgl2 bound to the aPKCiota-Par6B complex in nucleotide-free form. Conformation with visible head sub-complex.

Method: ELECTRON MICROSCOPY Dmax: 118.5 Å Quality: EXCELLENT

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

LLGL scribble cell polarity complex component 2

Homo sapiens

UniProt Q6P1M3

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 13–978 Not recorded Protein kinase C iota type × 1 (P41743) Partitioning defective 6 homolog beta × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.48 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.

9 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name L2GL2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–967; UniProt 13–978

Protein kinase C iota type

Homo sapiens

UniProt P41743

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–596 Non-standard monomer:Yes (specific site not provided by mmCIF) LLGL scribble cell polarity complex component 2 × 1 (Q6P1M3) Partitioning defective 6 homolog beta × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.48 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.

14 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KPCI_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–596; UniProt 1–596

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 9ejl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ejl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ejl
Deposition date deposition_date2024-11-28
Structure title titleLgl2 bound to the aPKCiota-Par6B complex in nucleotide-free form. Conformation with visible head sub-complex.
Keywords keywordsCell Polarity, Kinase, Complex., LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.63
Radius of gyration Rg (electron density) rg_electron37.81
Forward intensity I(0) i0409926000.00
Molecular weight molecular_weight166510.0 kDa
Excluded volume excluded_volume209170 ų
Envelope volume envelope_volume298210 ų
Hydration-shell volume shell_volume63840 ų
Envelope diameter envelope_diameter120.9
Shell Rg shell_rg45.60
Envelope Rg envelope_rg36.99
Shape Rg shape_rg37.84
Total Rg total_rg38.23
Total atoms total_atoms11764
Residues n_residues1562
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 dmax118.5
Rg (real space) rg_real38.36
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real4.0990e+08
I(0) uncertainty (real space) i0_real_error5.7970e+06
Rg (reciprocal space) rg_reciprocal38.53
I(0) (reciprocal space) i0_reciprocal410000000.0000
Solution quality estimate total_estimate0.9076
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.1
Skewness Skewness skewness0.064
Kurtosis Kurtosis kurtosis-0.667
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha94390000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.959

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)