4ph4

The crystal structure of Human VPS34 in complex with PIK-III

Method: X-RAY DIFFRACTION Dmax: 84.4 Å Quality: EXCELLENT

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 B; UniProt 293–887 Fragment:UNP residues 293-887 GOL GLYCEROL × 1 2UG 4'-(cyclopropylmethyl)-N~2~-(pyridin-4-yl)-4,5'-bipyrimidine-2,2'-diamine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;303.15 K;VPS34 protein and PIK-III were mixed and incubated on ice for 1 hr (final PIK-III concentration was 1 mM). Prior to crystallization, the mixture was passed through a 0.2 um filter. The protein:ligand complex was crystallized using the hanging drop vapor diffusion method in Nextal plates: 6 uL of protein solution was mixed with 4 uL of precipitant, which consisted of 20% (w/v) PEG 3350, 100 mM bis-tris propane, and 200 mM Na-K-phosphate. The resulting drop was suspended over a reservoir of 0.3 mL of precipitant and sealed with a screw cap. The crystals grew at 30 degC in approximately 12-24 hr. Resolution 2.80 Å R-free 0.223

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 31–625; UniProt 293–887

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 4ph4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ph4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ph4
Deposition date deposition_date2014-05-04
Structure title titleThe crystal structure of Human VPS34 in complex with PIK-III
Keywords keywordsVPS34, autophagy, class III, phosphatidylinositol-3-kinase, PIK3C3, TRANSFERASE-TRANSFERASE INHIBITOR complex; TRANSFERASE/TRANSFERASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.39
Radius of gyration Rg (electron density) rg_electron25.05
Forward intensity I(0) i058397500.00
Molecular weight molecular_weight60509.0 kDa
Excluded volume excluded_volume76255 ų
Envelope volume envelope_volume91524 ų
Hydration-shell volume shell_volume30277 ų
Envelope diameter envelope_diameter89.2
Shell Rg shell_rg32.57
Envelope Rg envelope_rg25.37
Shape Rg shape_rg25.06
Total Rg total_rg25.86
Total atoms total_atoms4258
Residues n_residues529
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_real26.30
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real5.8400e+07
I(0) uncertainty (real space) i0_real_error8.4140e+05
Rg (reciprocal space) rg_reciprocal26.33
I(0) (reciprocal space) i0_reciprocal58400000.0000
Solution quality estimate total_estimate0.9006
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.9
Skewness Skewness skewness0.239
Kurtosis Kurtosis kurtosis-0.424
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12450000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.965

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id4ph4B01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily70 — Phosphatidylinositol 3-kinase, accessory domain (PIK)
Domain ID domain_id4ph4B02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1010 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4
Homologous superfamily homologous superfamily10 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4
Domain ID domain_id4ph4B03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1070 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, Domain 5
Homologous superfamily homologous superfamily11 — Phosphatidylinositol 3-/4-kinase, catalytic domain

8. Citations (1)

9. Files and Curves (10)