3j4r

Pseudo-atomic model of the AKAP18-PKA Complex in a linear conformation derived from electron microscopy

Method: ELECTRON MICROSCOPY Dmax: 446.1 Å Quality: REASONABLE

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

cAMP-dependent protein kinase type II-alpha regulatory subunit

Mus musculus

UniProt Q8K1M3

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–402 Chain C; UniProt 1–402 Not recorded A-kinase anchor protein 18 × 1 cAMP-dependent protein kinase catalytic subunit alpha × 2 (P05132) ELECTRON MICROSCOPY cryo-EM buffer:25 mM HEPES, pH 7.4, 200 mM NaCl, 0.5 mM EDTA, 1 mM DTT;pH 7.4;25 mM HEPES, pH 7.4, 200 mM NaCl, 0.5 mM EDTA, 1 mM DTT Resolution 35.00 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.

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

View Construct and Data Evidence
UniProt name Q8K1M3_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–402; UniProt 1–402 Author chain C; PDBConstruct 1–402; UniProt 1–402

cAMP-dependent protein kinase catalytic subunit alpha

Mus musculus

UniProt P05132

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–351 Chain E; UniProt 1–351 Not recorded A-kinase anchor protein 18 × 1 cAMP-dependent protein kinase type II-alpha regulatory subunit × 2 (Q8K1M3) ELECTRON MICROSCOPY cryo-EM buffer:25 mM HEPES, pH 7.4, 200 mM NaCl, 0.5 mM EDTA, 1 mM DTT;pH 7.4;25 mM HEPES, pH 7.4, 200 mM NaCl, 0.5 mM EDTA, 1 mM DTT Resolution 35.00 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.

84 other PDB entries and 99 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAPCA_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–351; UniProt 1–351 Author chain E; PDBConstruct 1–351; UniProt 1–351

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 3j4r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j4r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3j4r
Deposition date deposition_date2013-09-25
Structure title titlePseudo-atomic model of the AKAP18-PKA Complex in a linear conformation derived from electron microscopy
Keywords keywords;A-kinase anchoring protein, cAMP-Dependent Kinase, RII, PKA regulatory subunit II, phosphorylation, anchoring, intrinsic disorder, TRANSFERASE ;; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron126.10
Forward intensity I(0) i0469172000.00
Molecular weight molecular_weight182800.0 kDa
Excluded volume excluded_volume229160 ų
Envelope volume envelope_volume602500 ų
Hydration-shell volume shell_volume54633 ų
Envelope diameter envelope_diameter390.0
Shell Rg shell_rg57.43
Envelope Rg envelope_rg113.10
Shape Rg shape_rg126.10
Total Rg total_rg124.90
Total atoms total_atoms12903
Residues n_residues1644
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 dmax446.1
Rg (real space) rg_real125.10
Rg uncertainty (real space) rg_real_error7.50
I(0) (real space) i0_real4.6940e+08
I(0) uncertainty (real space) i0_real_error1.3670e+07
Rg (reciprocal space) rg_reciprocal92.37
I(0) (reciprocal space) i0_reciprocal426400000.0000
Solution quality estimate total_estimate0.5702
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary37.2
Skewness Skewness skewness0.356
Kurtosis Kurtosis kurtosis-1.246
Angular range angular_range— – 0.0600 −1
Current regularization parameter α current_alpha0.0735
Highest regularization parameter α highest_alpha23200000.0000
Real-space data points n_real_points13
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.000; Stabil: 0.816; Sysdev: 1.000; Positv: 1.000; Valcen: 0.001; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)