4ntt

Structure of the catalytic subunit of cAMP-dependent protein kinase bound to ADP and one magnesium ion

Method: X-RAY DIFFRACTION Dmax: 112.2 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–351 Mutation:K7C Non-standard monomer:Yes (specific site not provided by mmCIF) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277.15 K;8% MPD, 0.1 M Bicine, 150 mM Ammonium Acetate, 10 mM DTT, 9% methanol added to the well, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K Resolution 3.50 Å R-free 0.284
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2–351 Mutation:K7C Non-standard monomer:Yes (specific site not provided by mmCIF) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277.15 K;8% MPD, 0.1 M Bicine, 150 mM Ammonium Acetate, 10 mM DTT, 9% methanol added to the well, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K Resolution 3.50 Å R-free 0.284

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 98 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 A; PDBConstruct 1–350; UniProt 2–351 Author chain B; PDBConstruct 1–350; UniProt 2–351

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 4ntt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4ntt
Deposition date deposition_date2013-12-02
Structure title titleStructure of the catalytic subunit of cAMP-dependent protein kinase bound to ADP and one magnesium ion
Keywords keywordsprotein kinase fold, kinase, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.78
Radius of gyration Rg (electron density) rg_electron33.23
Forward intensity I(0) i087376000.00
Molecular weight molecular_weight74315.0 kDa
Excluded volume excluded_volume92746 ų
Envelope volume envelope_volume124260 ų
Hydration-shell volume shell_volume32563 ų
Envelope diameter envelope_diameter120.1
Shell Rg shell_rg37.93
Envelope Rg envelope_rg33.02
Shape Rg shape_rg33.18
Total Rg total_rg33.78
Total atoms total_atoms5262
Residues n_residues678
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 dmax112.2
Rg (real space) rg_real33.99
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real8.7380e+07
I(0) uncertainty (real space) i0_real_error1.2190e+06
Rg (reciprocal space) rg_reciprocal33.86
I(0) (reciprocal space) i0_reciprocal87370000.0000
Solution quality estimate total_estimate0.8414
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.449
Kurtosis Kurtosis kurtosis-0.525
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25180000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.800; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.728; Smooth: 0.806

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4nttA01
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_id4nttA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id4nttB01
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_id4nttB02
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)