8t15

Cryo-EM structure of dodecameric hub domain of CaMKII alpha

Method: ELECTRON MICROSCOPY Dmax: 118.4 Å Quality: GOOD

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

Venus-tagged CaMKII Alpha Association Domain

Rattus norvegicus

UniProt P11275

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 345–478 Chain B; UniProt 345–478 Chain C; UniProt 345–478 Chain D; UniProt 345–478 Chain E; UniProt 345–478 Chain F; UniProt 345–478 Chain G; UniProt 345–478 Chain H; UniProt 345–478 Chain I; UniProt 345–478 Chain J; UniProt 345–478 Chain K; UniProt 345–478 Chain L; UniProt 345–478 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

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

View Construct and Data Evidence
UniProt name KCC2A_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 274–407; UniProt 345–478 Author chain B; PDBConstruct 274–407; UniProt 345–478 Author chain C; PDBConstruct 274–407; UniProt 345–478 Author chain D; PDBConstruct 274–407; UniProt 345–478 Author chain E; PDBConstruct 274–407; UniProt 345–478 Author chain F; PDBConstruct 274–407; UniProt 345–478 Author chain G; PDBConstruct 274–407; UniProt 345–478 Author chain H; PDBConstruct 274–407; UniProt 345–478 Author chain I; PDBConstruct 274–407; UniProt 345–478 Author chain J; PDBConstruct 274–407; UniProt 345–478 Author chain K; PDBConstruct 274–407; UniProt 345–478 Author chain L; PDBConstruct 274–407; UniProt 345–478

Venus-tagged CaMKII Alpha Association Domain

Rattus norvegicus

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 2–238 Chain B; UniProt 2–238 Chain C; UniProt 2–238 Chain D; UniProt 2–238 Chain E; UniProt 2–238 Chain F; UniProt 2–238 Chain G; UniProt 2–238 Chain H; UniProt 2–238 Chain I; UniProt 2–238 Chain J; UniProt 2–238 Chain K; UniProt 2–238 Chain L; UniProt 2–238 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 22–258; UniProt 2–238 Author chain B; PDBConstruct 22–258; UniProt 2–238 Author chain C; PDBConstruct 22–258; UniProt 2–238 Author chain D; PDBConstruct 22–258; UniProt 2–238 Author chain E; PDBConstruct 22–258; UniProt 2–238 Author chain F; PDBConstruct 22–258; UniProt 2–238 Author chain G; PDBConstruct 22–258; UniProt 2–238 Author chain H; PDBConstruct 22–258; UniProt 2–238 Author chain I; PDBConstruct 22–258; UniProt 2–238 Author chain J; PDBConstruct 22–258; UniProt 2–238 Author chain K; PDBConstruct 22–258; UniProt 2–238 Author chain L; PDBConstruct 22–258; UniProt 2–238

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 8t15

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t15
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8t15
Deposition date deposition_date2023-06-01
Structure title titleCryo-EM structure of dodecameric hub domain of CaMKII alpha
Keywords keywordsHigh-order oligomer, Protein Kinase, Signaling, Memory, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.48
Radius of gyration Rg (electron density) rg_electron38.50
Forward intensity I(0) i0535336000.00
Molecular weight molecular_weight184790.0 kDa
Excluded volume excluded_volume229740 ų
Envelope volume envelope_volume321090 ų
Hydration-shell volume shell_volume68170 ų
Envelope diameter envelope_diameter115.7
Shell Rg shell_rg46.13
Envelope Rg envelope_rg36.70
Shape Rg shape_rg38.45
Total Rg total_rg39.12
Total atoms total_atoms25656
Residues n_residues1608
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 dmax118.4
Rg (real space) rg_real39.15
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real5.3530e+08
I(0) uncertainty (real space) i0_real_error8.3720e+06
Rg (reciprocal space) rg_reciprocal39.36
I(0) (reciprocal space) i0_reciprocal535500000.0000
Solution quality estimate total_estimate0.8994
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.3
Skewness Skewness skewness0.005
Kurtosis Kurtosis kurtosis-0.611
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40600000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.867

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)