8ukn

APO and AMP-PNP bound cAMP-dependent protein kinase A catalytic domain

Method: X-RAY DIFFRACTION Dmax: 123.1 Å Quality: EXCELLENT

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 16–351 Non-standard monomer:Yes (specific site not provided by mmCIF) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277.115 K;0.1 M HEPES pH 7.5, 10% (w/v) PEG 8000 Resolution 2.75 Å R-free 0.232
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 16–351 Non-standard monomer:Yes (specific site not provided by mmCIF) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277.115 K;0.1 M HEPES pH 7.5, 10% (w/v) PEG 8000 Resolution 2.75 Å R-free 0.232
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain F; UniProt 16–351 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277.115 K;0.1 M HEPES pH 7.5, 10% (w/v) PEG 8000 Resolution 2.75 Å R-free 0.232
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain H; UniProt 16–351 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277.115 K;0.1 M HEPES pH 7.5, 10% (w/v) PEG 8000 Resolution 2.75 Å R-free 0.232

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 96 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAPCA_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 4–339; UniProt 16–351 Author chain D; PDBConstruct 4–339; UniProt 16–351 Author chain F; PDBConstruct 4–339; UniProt 16–351 Author chain H; PDBConstruct 4–339; UniProt 16–351

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 8ukn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ukn
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8ukn
Deposition date deposition_date2023-10-14
Structure title titleAPO and AMP-PNP bound cAMP-dependent protein kinase A catalytic domain
Keywords keywordsProtein Kinase, Complex, Ion Channel, Voltage gated calcium channel, Cardiac channel, Stress signaling, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.40
Radius of gyration Rg (electron density) rg_electron38.66
Forward intensity I(0) i0318360000.00
Molecular weight molecular_weight150310.0 kDa
Excluded volume excluded_volume190090 ų
Envelope volume envelope_volume260090 ų
Hydration-shell volume shell_volume55202 ų
Envelope diameter envelope_diameter127.2
Shell Rg shell_rg45.68
Envelope Rg envelope_rg37.57
Shape Rg shape_rg38.65
Total Rg total_rg39.14
Total atoms total_atoms10618
Residues n_residues1287
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 dmax123.1
Rg (real space) rg_real39.20
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real3.1840e+08
I(0) uncertainty (real space) i0_real_error5.4890e+06
Rg (reciprocal space) rg_reciprocal39.33
I(0) (reciprocal space) i0_reciprocal318400000.0000
Solution quality estimate total_estimate0.9077
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.3
Skewness Skewness skewness0.101
Kurtosis Kurtosis kurtosis-0.633
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha47210000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.933

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)