9rx5

VPS34-CII (VPS34 199-REIE-202 to 199-AAAA-202 mutant) bound to RAB5A (Q79L)

Method: ELECTRON MICROSCOPY Dmax: 213.3 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–887 Mutation:199-REIE-202 to 199-AAAA-202 Phosphoinositide 3-kinase regulatory subunit 4 × 1 (Q99570) Beclin-1 × 1 (Q14457) UV radiation resistance associated protein × 1 (Q6P1X0) Ras-related protein Rab-5A × 2 (P20339) MYRISTIC ACID × 1 GUANOSINE-5'-DIPHOSPHATE × 1 MAGNESIUM ION × 3 ZINC ION × 1 GUANOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.15 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 A; PDBConstruct 1–887; UniProt 1–887

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 2–1358 Not recorded Phosphatidylinositol 3-kinase catalytic subunit type 3 × 1 (Q8NEB9) Beclin-1 × 1 (Q14457) UV radiation resistance associated protein × 1 (Q6P1X0) Ras-related protein Rab-5A × 2 (P20339) MYRISTIC ACID × 1 GUANOSINE-5'-DIPHOSPHATE × 1 MAGNESIUM ION × 3 ZINC ION × 1 GUANOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.15 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1357; UniProt 2–1358

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–450 Not recorded Phosphatidylinositol 3-kinase catalytic subunit type 3 × 1 (Q8NEB9) Phosphoinositide 3-kinase regulatory subunit 4 × 1 (Q99570) UV radiation resistance associated protein × 1 (Q6P1X0) Ras-related protein Rab-5A × 2 (P20339) MYRISTIC ACID × 1 GUANOSINE-5'-DIPHOSPHATE × 1 MAGNESIUM ION × 3 ZINC ION × 1 GUANOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.15 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 C; PDBConstruct 1–450; UniProt 1–450

UV radiation resistance associated protein

Homo sapiens

UniProt Q6P1X0

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 1–699 Mutation:P10Q Phosphatidylinositol 3-kinase catalytic subunit type 3 × 1 (Q8NEB9) Phosphoinositide 3-kinase regulatory subunit 4 × 1 (Q99570) Beclin-1 × 1 (Q14457) Ras-related protein Rab-5A × 2 (P20339) MYRISTIC ACID × 1 GUANOSINE-5'-DIPHOSPHATE × 1 MAGNESIUM ION × 3 ZINC ION × 1 GUANOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.15 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.

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

View Construct and Data Evidence
UniProt name Q6P1X0_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–699; UniProt 1–699

Ras-related protein Rab-5A

Homo sapiens

UniProt P20339

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 1–212 Chain F; UniProt 1–212 Mutation:C19A, C63S, Q79L Phosphatidylinositol 3-kinase catalytic subunit type 3 × 1 (Q8NEB9) Phosphoinositide 3-kinase regulatory subunit 4 × 1 (Q99570) Beclin-1 × 1 (Q14457) UV radiation resistance associated protein × 1 (Q6P1X0) MYRISTIC ACID × 1 GUANOSINE-5'-DIPHOSPHATE × 1 MAGNESIUM ION × 3 ZINC ION × 1 GUANOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.15 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.

19 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAB5A_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–212; UniProt 1–212 Author chain F; PDBConstruct 1–212; UniProt 1–212

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 9rx5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9rx5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9rx5
Deposition date deposition_date2025-07-10
Structure title titleVPS34-CII (VPS34 199-REIE-202 to 199-AAAA-202 mutant) bound to RAB5A (Q79L)
Keywords keywordsLipid kinase, GTPase, kinase, autophagy, endocytic trafficking, SIGNALING PROTEIN, ENDOCYTOSIS; ENDOCYTOSIS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier67.73
Radius of gyration Rg (electron density) rg_electron68.20
Forward intensity I(0) i01811170000.00
Molecular weight molecular_weight361420.0 kDa
Excluded volume excluded_volume453880 ų
Envelope volume envelope_volume751320 ų
Hydration-shell volume shell_volume97729 ų
Envelope diameter envelope_diameter244.1
Shell Rg shell_rg62.21
Envelope Rg envelope_rg66.80
Shape Rg shape_rg68.22
Total Rg total_rg67.99
Total atoms total_atoms25422
Residues n_residues3150
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 dmax213.3
Rg (real space) rg_real67.94
Rg uncertainty (real space) rg_real_error1.74
I(0) (real space) i0_real1.8110e+09
I(0) uncertainty (real space) i0_real_error3.8670e+07
Rg (reciprocal space) rg_reciprocal66.66
I(0) (reciprocal space) i0_reciprocal1807000000.0000
Solution quality estimate total_estimate0.8258
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.6
Skewness Skewness skewness0.427
Kurtosis Kurtosis kurtosis-0.487
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0004
Highest regularization parameter α highest_alpha150300000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.941; Smooth: 0.024

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (2)

9. Files and Curves (10)