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8ds6

Structure of the PEAK3 pseudokinase homodimer

Method: ELECTRON MICROSCOPY Dmax: 103.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Protein PEAK3

Homo sapiens

UniProt Q6ZS72

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 1–473 Chain B； UniProt 1–473 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；A final concentration of 0.1% of Octyl-beta-Glucoside (C14H28O6) was added to the sample before freezing. cryo-EM vitrification conditions：Cryogen ETHANE；blot time = 7s blot force = 4 Resolution 4.90 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.

Other PDB Difference from Current Entry 8DS6 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8DP5 Structure of the PEAK3/14-3-3 complex Deposited 2022-07-14 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 1–473（473 aa）
Chain B 1–473（473 aa）
Chain E 1–473（473 aa）
Chain P 1–473（473 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；A final concentration of 0.1% of Octyl-beta-Glucoside (C14H28O6) was added to the sample before freezing.
cryo-EM vitrification conditions Cryogen ETHANE；blot time = 7s blot force = 4
Resolution 3.10 Å

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

View Construct and Data Evidence
UniProt name PEAK3_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–473； UniProt 1–473 Author chain B； PDBConstruct 1–473； UniProt 1–473

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 8ds6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ds6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ds6
Deposition date deposition_date2022-07-21
Structure title titleStructure of the PEAK3 pseudokinase homodimer
Keywords keywordscomplex, pseudokinase, kinase, adapter, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier32.67 Å
Radius of gyration Rg (electron density) rg_electron32.16 Å
Forward intensity I(0) i077464800.00
Molecular weight molecular_weight71246.0 kDa
Excluded volume excluded_volume90038 ų
Envelope volume envelope_volume120140 ų
Hydration-shell volume shell_volume31844 ų
Envelope diameter envelope_diameter100.1 Å
Shell Rg shell_rg38.42 Å
Envelope Rg envelope_rg31.50 Å
Shape Rg shape_rg32.19 Å
Total Rg total_rg32.65 Å
Total atoms total_atoms10135
Residues n_residues669
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax103.8 Å
Rg (real space) rg_real32.72 Å
Rg uncertainty (real space) rg_real_error0.94 Å
I(0) (real space) i0_real7.7460e+07
I(0) uncertainty (real space) i0_real_error1.3930e+06
Rg (reciprocal space) rg_reciprocal32.70 Å
I(0) (reciprocal space) i0_reciprocal77460000.0000
Solution quality estimate total_estimate0.8964
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.3 Å
Skewness Skewness skewness0.242
Kurtosis Kurtosis kurtosis-0.779
Angular range angular_range— – 0.2400 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12690000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.932; Smooth: 0.953
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)