13bv

Cryo-EM structure of human PI3KC3-C1 complex

Method: ELECTRON MICROSCOPY Dmax: 206.7 Å Quality: GOOD

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

Phosphatidylinositol 3-kinase catalytic subunit type 3

Homo sapiens

UniProt Q8NEB9

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 B; UniProt 1–887 Not recorded Beclin 1-associated autophagy-related key regulator × 1 (Q6ZNE5) Beclin-1 × 1 (Q14457) Phosphoinositide 3-kinase regulatory subunit 4 × 1 (Q99570) MYR MYRISTIC ACID × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.77 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.

40 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PK3C3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–887; UniProt 1–887

Beclin 1-associated autophagy-related key regulator

Homo sapiens

UniProt Q6ZNE5

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 C; UniProt 1–492 Not recorded Phosphatidylinositol 3-kinase catalytic subunit type 3 × 1 (Q8NEB9) Beclin-1 × 1 (Q14457) Phosphoinositide 3-kinase regulatory subunit 4 × 1 (Q99570) MYR MYRISTIC ACID × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.77 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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAKOR_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–492; UniProt 1–492

Beclin-1

Homo sapiens

UniProt Q14457

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 D; UniProt 1–450 Not recorded Phosphatidylinositol 3-kinase catalytic subunit type 3 × 1 (Q8NEB9) Beclin 1-associated autophagy-related key regulator × 1 (Q6ZNE5) Phosphoinositide 3-kinase regulatory subunit 4 × 1 (Q99570) MYR MYRISTIC ACID × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.77 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.

29 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BECN1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–450; UniProt 1–450

Phosphoinositide 3-kinase regulatory subunit 4

Homo sapiens

UniProt Q99570

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 A; UniProt 1–1358 Not recorded Phosphatidylinositol 3-kinase catalytic subunit type 3 × 1 (Q8NEB9) Beclin 1-associated autophagy-related key regulator × 1 (Q6ZNE5) Beclin-1 × 1 (Q14457) MYR MYRISTIC ACID × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.77 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PI3R4_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain A; PDBConstruct 1–1358; UniProt 1–1358

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 13bv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 13bv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id13bv
Deposition date deposition_date2026-04-28
最后修订 last_revision2026-05-13
Structure title titleCryo-EM structure of human PI3KC3-C1 complex
Keywords keywordsLipid kinase, autophagosome formation, signaling protein, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier58.17
Radius of gyration Rg (electron density) rg_electron58.68
Forward intensity I(0) i0726853000.00
Molecular weight molecular_weight227360.0 kDa
Excluded volume excluded_volume285490 ų
Envelope volume envelope_volume421660 ų
Hydration-shell volume shell_volume63851 ų
Envelope diameter envelope_diameter205.1
Shell Rg shell_rg55.17
Envelope Rg envelope_rg57.44
Shape Rg shape_rg58.70
Total Rg total_rg58.52
Total atoms total_atoms15991
Residues n_residues1976
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 dmax206.7
Rg (real space) rg_real58.53
Rg uncertainty (real space) rg_real_error2.61
I(0) (real space) i0_real7.2690e+08
I(0) uncertainty (real space) i0_real_error1.5490e+07
Rg (reciprocal space) rg_reciprocal57.83
I(0) (reciprocal space) i0_reciprocal726000000.0000
Solution quality estimate total_estimate0.7630
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.3
Skewness Skewness skewness0.342
Kurtosis Kurtosis kurtosis-0.587
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha31390000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.743; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.687; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)