8dwt

SPOP W22R Form 2

Method: ELECTRON MICROSCOPY Dmax: 226.4 Å Quality: GOOD

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

Speckle-type POZ protein

Homo sapiens

UniProt O43791

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 2–374 Chain B; UniProt 2–374 Chain C; UniProt 2–374 Chain D; UniProt 2–374 Chain E; UniProt 2–374 Chain F; UniProt 2–374 Chain G; UniProt 2–374 Chain H; UniProt 2–374 Chain I; UniProt 2–374 Chain J; UniProt 2–374 Chain K; UniProt 2–374 Chain L; UniProt 2–374 Mutation:W22R No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 400 mM NaCl, 5 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.20 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.

34 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPOP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–373; UniProt 2–374 Author chain B; PDBConstruct 1–373; UniProt 2–374 Author chain C; PDBConstruct 1–373; UniProt 2–374 Author chain D; PDBConstruct 1–373; UniProt 2–374 Author chain E; PDBConstruct 1–373; UniProt 2–374 Author chain F; PDBConstruct 1–373; UniProt 2–374 Author chain G; PDBConstruct 1–373; UniProt 2–374 Author chain H; PDBConstruct 1–373; UniProt 2–374 Author chain I; PDBConstruct 1–373; UniProt 2–374 Author chain J; PDBConstruct 1–373; UniProt 2–374 Author chain K; PDBConstruct 1–373; UniProt 2–374 Author chain L; PDBConstruct 1–373; UniProt 2–374

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 8dwt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8dwt
Deposition date deposition_date2022-08-02
Structure title titleSPOP W22R Form 2
Keywords keywordsSPOP, ubiquitination, cullin, ONCOPROTEIN; ONCOPROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier74.86
Radius of gyration Rg (electron density) rg_electron75.46
Forward intensity I(0) i03128700000.00
Molecular weight molecular_weight468620.0 kDa
Excluded volume excluded_volume585030 ų
Envelope volume envelope_volume1017200 ų
Hydration-shell volume shell_volume120380 ų
Envelope diameter envelope_diameter277.1
Shell Rg shell_rg63.57
Envelope Rg envelope_rg74.31
Shape Rg shape_rg75.45
Total Rg total_rg75.26
Total atoms total_atoms32810
Residues n_residues4176
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 dmax226.4
Rg (real space) rg_real74.38
Rg uncertainty (real space) rg_real_error1.36
I(0) (real space) i0_real3.1090e+09
I(0) uncertainty (real space) i0_real_error5.7560e+07
Rg (reciprocal space) rg_reciprocal72.60
I(0) (reciprocal space) i0_reciprocal3111000000.0000
Solution quality estimate total_estimate0.7928
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary64.7
Skewness Skewness skewness0.540
Kurtosis Kurtosis kurtosis-0.454
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0300
Highest regularization parameter α highest_alpha1151000000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.757; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.030

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)