8r3y

Cryo EM structure of a stable LGL/aPKC Iota/Par-6 complex

Method: ELECTRON MICROSCOPY Dmax: 109.0 Å Quality: EXCELLENT

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

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 I; UniProt 248–585 Non-standard monomer:Yes (specific site not provided by mmCIF) Lethal(2) giant larvae protein homolog 1 × 1 (Q15334) Partitioning defective 6 homolog alpha × 1 (Q9NPB6) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;4 ul of aPKCiota-Par6-Llgl1 complex at a concentration of 0.4 mg/ml was applied to R1.2/1.3 Quantifoil 300 mesh copper grids which had been glow-discharged for 45 s at 45 mA . Grids were blotted for 2.5 s at 100% humidity using an FEI Vitrobot MK IV. Resolution 3.68 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 1
Chains and sequence ranges Author chain I; PDBConstruct 1–338; UniProt 248–585

Lethal(2) giant larvae protein homolog 1

Homo sapiens

UniProt Q15334

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 L; UniProt 15–951 Non-standard monomer:Yes (specific site not provided by mmCIF) Protein kinase C iota type × 1 (P41743) Partitioning defective 6 homolog alpha × 1 (Q9NPB6) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;4 ul of aPKCiota-Par6-Llgl1 complex at a concentration of 0.4 mg/ml was applied to R1.2/1.3 Quantifoil 300 mesh copper grids which had been glow-discharged for 45 s at 45 mA . Grids were blotted for 2.5 s at 100% humidity using an FEI Vitrobot MK IV. Resolution 3.68 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name L2GL1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 1–937; UniProt 15–951

Partitioning defective 6 homolog alpha

Homo sapiens

UniProt Q9NPB6

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 P; UniProt 154–252 Not recorded Protein kinase C iota type × 1 (P41743) Lethal(2) giant larvae protein homolog 1 × 1 (Q15334) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;4 ul of aPKCiota-Par6-Llgl1 complex at a concentration of 0.4 mg/ml was applied to R1.2/1.3 Quantifoil 300 mesh copper grids which had been glow-discharged for 45 s at 45 mA . Grids were blotted for 2.5 s at 100% humidity using an FEI Vitrobot MK IV. Resolution 3.68 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PAR6A_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 1–99; UniProt 154–252

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 8r3y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8r3y
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8r3y
Deposition date deposition_date2023-11-10
Structure title titleCryo EM structure of a stable LGL/aPKC Iota/Par-6 complex
Keywords keywordsKinase, Polarity, Kinase substrate complex., CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.15
Radius of gyration Rg (electron density) rg_electron34.33
Forward intensity I(0) i0321529000.00
Molecular weight molecular_weight143870.0 kDa
Excluded volume excluded_volume179850 ų
Envelope volume envelope_volume239010 ų
Hydration-shell volume shell_volume56063 ų
Envelope diameter envelope_diameter113.3
Shell Rg shell_rg42.37
Envelope Rg envelope_rg34.16
Shape Rg shape_rg34.34
Total Rg total_rg34.89
Total atoms total_atoms20120
Residues n_residues1290
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 dmax109.0
Rg (real space) rg_real34.99
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real3.2150e+08
I(0) uncertainty (real space) i0_real_error4.7850e+06
Rg (reciprocal space) rg_reciprocal35.09
I(0) (reciprocal space) i0_reciprocal321600000.0000
Solution quality estimate total_estimate0.9044
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.2
Skewness Skewness skewness0.159
Kurtosis Kurtosis kurtosis-0.564
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha83400000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.939

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)