9orm

The structure of human Vacuolar Protein Sorting 34 catalytic domain bound to RD-I-137

Method: X-RAY DIFFRACTION Dmax: 84.4 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 290–871 Not recorded A1CD6 ethyl 2-[(8S)-pyrazolo[1,5-a]pyrimidin-3-yl]-1,3-benzothiazole-6-carboxylate × 1 GOL GLYCEROL × 2 PEG DI(HYDROXYETHYL)ETHER × 2 CL CHLORIDE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6;298 K;0.1 M Ammonium acetate, 0.1 M BIS-TRIS pH 5.5, 17% w/v Polyethylene glycol 10,000 Resolution 2.06 Å R-free 0.227

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 13–594; UniProt 290–871

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 9orm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9orm
Deposition date deposition_date2025-05-22
最后修订 last_revision2026-04-15
Structure title titleThe structure of human Vacuolar Protein Sorting 34 catalytic domain bound to RD-I-137
Keywords keywordsPhosophatidylinositol-3-Phosphate, lipid regulator, autophagy, membrane trafficking, endocytosis, enzyme, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.96
Radius of gyration Rg (electron density) rg_electron25.09
Forward intensity I(0) i0115723000.00
Molecular weight molecular_weight57025.0 kDa
Excluded volume excluded_volume55406 ų
Envelope volume envelope_volume91491 ų
Hydration-shell volume shell_volume30318 ų
Envelope diameter envelope_diameter88.2
Shell Rg shell_rg32.46
Envelope Rg envelope_rg25.32
Shape Rg shape_rg25.07
Total Rg total_rg25.70
Total atoms total_atoms4344
Residues n_residues533
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 dmax84.4
Rg (real space) rg_real25.89
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real1.1570e+08
I(0) uncertainty (real space) i0_real_error1.4370e+06
Rg (reciprocal space) rg_reciprocal25.91
I(0) (reciprocal space) i0_reciprocal115700000.0000
Solution quality estimate total_estimate0.8981
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.4
Skewness Skewness skewness0.257
Kurtosis Kurtosis kurtosis-0.410
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19420000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)