7lz4

Crystal structure of A211D mutant of Protein Kinase A RIa subunit, a Carney Complex mutation

Method: X-RAY DIFFRACTION Dmax: 151.6 Å Quality: GOOD

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

cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed

Bos taurus

UniProt P00514

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 A; UniProt 109–377 Mutation:A211D CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295.5 K;The protein was concentrated to 8 mg/mL, and crystallized in 2 uL hanging drops using the vapor diffusion method with 75 mM Sodium Acetate (pH 5.0), 2.0 M sodium formate, and four-fold molar excess cAMP at room temperature Resolution 4.16 Å R-free 0.270
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 109–377 Mutation:A211D CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295.5 K;The protein was concentrated to 8 mg/mL, and crystallized in 2 uL hanging drops using the vapor diffusion method with 75 mM Sodium Acetate (pH 5.0), 2.0 M sodium formate, and four-fold molar excess cAMP at room temperature Resolution 4.16 Å R-free 0.270
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 109–377 Mutation:A211D CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295.5 K;The protein was concentrated to 8 mg/mL, and crystallized in 2 uL hanging drops using the vapor diffusion method with 75 mM Sodium Acetate (pH 5.0), 2.0 M sodium formate, and four-fold molar excess cAMP at room temperature Resolution 4.16 Å R-free 0.270
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 109–377 Mutation:A211D CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295.5 K;The protein was concentrated to 8 mg/mL, and crystallized in 2 uL hanging drops using the vapor diffusion method with 75 mM Sodium Acetate (pH 5.0), 2.0 M sodium formate, and four-fold molar excess cAMP at room temperature Resolution 4.16 Å R-free 0.270
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 109–377 Mutation:A211D CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295.5 K;The protein was concentrated to 8 mg/mL, and crystallized in 2 uL hanging drops using the vapor diffusion method with 75 mM Sodium Acetate (pH 5.0), 2.0 M sodium formate, and four-fold molar excess cAMP at room temperature Resolution 4.16 Å R-free 0.270
6 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain F; UniProt 109–377 Mutation:A211D CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295.5 K;The protein was concentrated to 8 mg/mL, and crystallized in 2 uL hanging drops using the vapor diffusion method with 75 mM Sodium Acetate (pH 5.0), 2.0 M sodium formate, and four-fold molar excess cAMP at room temperature Resolution 4.16 Å R-free 0.270
7 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain G; UniProt 109–377 Mutation:A211D CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295.5 K;The protein was concentrated to 8 mg/mL, and crystallized in 2 uL hanging drops using the vapor diffusion method with 75 mM Sodium Acetate (pH 5.0), 2.0 M sodium formate, and four-fold molar excess cAMP at room temperature Resolution 4.16 Å R-free 0.270
8 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain H; UniProt 109–377 Mutation:A211D CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295.5 K;The protein was concentrated to 8 mg/mL, and crystallized in 2 uL hanging drops using the vapor diffusion method with 75 mM Sodium Acetate (pH 5.0), 2.0 M sodium formate, and four-fold molar excess cAMP at room temperature Resolution 4.16 Å R-free 0.270

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.

25 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAP0_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–269; UniProt 109–377 Author chain B; PDBConstruct 1–269; UniProt 109–377 Author chain C; PDBConstruct 1–269; UniProt 109–377 Author chain D; PDBConstruct 1–269; UniProt 109–377 Author chain E; PDBConstruct 1–269; UniProt 109–377 Author chain F; PDBConstruct 1–269; UniProt 109–377 Author chain G; PDBConstruct 1–269; UniProt 109–377 Author chain H; PDBConstruct 1–269; UniProt 109–377

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 7lz4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7lz4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7lz4
Deposition date deposition_date2021-03-08
Structure title titleCrystal structure of A211D mutant of Protein Kinase A RIa subunit, a Carney Complex mutation
Keywords keywordsCarney complex, cyclic nucleotide binding domain, cyclic AMP (cAMP), protein kinase A (PKA), TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier46.99
Radius of gyration Rg (electron density) rg_electron46.37
Forward intensity I(0) i0883155000.00
Molecular weight molecular_weight243480.0 kDa
Excluded volume excluded_volume303800 ų
Envelope volume envelope_volume440420 ų
Hydration-shell volume shell_volume79139 ų
Envelope diameter envelope_diameter154.2
Shell Rg shell_rg51.44
Envelope Rg envelope_rg44.74
Shape Rg shape_rg46.37
Total Rg total_rg46.56
Total atoms total_atoms17138
Residues n_residues2142
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 dmax151.6
Rg (real space) rg_real46.83
Rg uncertainty (real space) rg_real_error1.35
I(0) (real space) i0_real8.8320e+08
I(0) uncertainty (real space) i0_real_error1.4970e+07
Rg (reciprocal space) rg_reciprocal46.99
I(0) (reciprocal space) i0_reciprocal883300000.0000
Solution quality estimate total_estimate0.8028
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.0
Skewness Skewness skewness0.247
Kurtosis Kurtosis kurtosis-0.326
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40170000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.819; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)