4dfx

Crystal structure of myristoylated K7C catalytic subunit of cAMP-dependent protein kinase in complex with SP20 and AMP-PNP

Method: X-RAY DIFFRACTION Dmax: 68.3 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 2–351 Fragment:UNP RESIDUES 2-351 Mutation:K7C Non-standard monomer:Yes (specific site not provided by mmCIF) cAMP-dependent protein kinase inhibitor alpha × 1 (P63248) MYR MYRISTIC ACID × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 2 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277.15 K;Mother liquor: 12% MPD, 100 mM Bis-Tris, Protein solution: 50 mM Bicine, 150 mM Ammonium Acetate, 10 mM DTT, 8-10 mg/mL 9% MeOH added to the well immediately before sealing. 8 uL drop size with 1:1 protein:mother liquor, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K, pH 8.0 Resolution 1.35 Å R-free 0.179

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 1
Chains and sequence ranges Author chain E; PDBConstruct 1–350; UniProt 2–351

cAMP-dependent protein kinase inhibitor alpha

OrganismNot specified

UniProt P63248

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 6–25 Fragment:UNP RESIDUES 6-25 Mutation:N20A, A21S cAMP-dependent protein kinase catalytic subunit alpha × 1 (P05132) MYR MYRISTIC ACID × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 2 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277.15 K;Mother liquor: 12% MPD, 100 mM Bis-Tris, Protein solution: 50 mM Bicine, 150 mM Ammonium Acetate, 10 mM DTT, 8-10 mg/mL 9% MeOH added to the well immediately before sealing. 8 uL drop size with 1:1 protein:mother liquor, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K, pH 8.0 Resolution 1.35 Å R-free 0.179

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.

46 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IPKA_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–20; UniProt 6–25

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 4dfx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4dfx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4dfx
Deposition date deposition_date2012-01-24
Structure title titleCrystal structure of myristoylated K7C catalytic subunit of cAMP-dependent protein kinase in complex with SP20 and AMP-PNP
Keywords keywords;Protein kinase, myristoylated, Phosphotransferase onto Ser/Thr, Mg, PKI, PKA Regulatory subunits, phosphorylated on S139, T197, S338, myristoylated on G1, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR complex ;; TRANSFERASE/TRANSFERASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.69
Radius of gyration Rg (electron density) rg_electron20.39
Forward intensity I(0) i031656300.00
Molecular weight molecular_weight43738.0 kDa
Excluded volume excluded_volume54940 ų
Envelope volume envelope_volume62863 ų
Hydration-shell volume shell_volume24906 ų
Envelope diameter envelope_diameter72.2
Shell Rg shell_rg27.82
Envelope Rg envelope_rg20.72
Shape Rg shape_rg20.35
Total Rg total_rg21.44
Total atoms total_atoms3081
Residues n_residues367
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 dmax68.3
Rg (real space) rg_real21.55
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real3.1660e+07
I(0) uncertainty (real space) i0_real_error3.7500e+05
Rg (reciprocal space) rg_reciprocal21.58
I(0) (reciprocal space) i0_reciprocal31660000.0000
Solution quality estimate total_estimate0.8964
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.5
Skewness Skewness skewness0.183
Kurtosis Kurtosis kurtosis-0.397
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8135000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.887; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4dfxE01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id4dfxE02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1

8. Citations (1)

9. Files and Curves (10)