3pvb

Crystal structure of (73-244)RIa:C holoenzyme of cAMP-dependent Protein kinase

Method: X-RAY DIFFRACTION Dmax: 82.7 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 A; UniProt 7–351 Fragment:unp residues 7-351 Non-standard monomer:Yes (specific site not provided by mmCIF) cAMP-dependent protein kinase type I-alpha regulatory subunit × 1 (P00514) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MN MANGANESE (II) ION × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;298 K;The RIa(73-244):C complex was crystallized in 0.1M MES pH 6.0 and 12% PEG 20,000 by using a Douglas Instruments Oryx8 crystallography robot as 1:1 protein solution:crystallizing solution, VAPOR DIFFUSION, SITTING DROP, temperature 298.0 K Resolution 3.30 Å R-free 0.290

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 A; PDBConstruct 1–345; UniProt 7–351

cAMP-dependent protein kinase type I-alpha regulatory subunit

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 85–244 Fragment:unp residues 85-244 cAMP-dependent protein kinase catalytic subunit alpha × 1 (P05132) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MN MANGANESE (II) ION × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;298 K;The RIa(73-244):C complex was crystallized in 0.1M MES pH 6.0 and 12% PEG 20,000 by using a Douglas Instruments Oryx8 crystallography robot as 1:1 protein solution:crystallizing solution, VAPOR DIFFUSION, SITTING DROP, temperature 298.0 K Resolution 3.30 Å R-free 0.290

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 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAP0_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–160; UniProt 85–244

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 3pvb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3pvb
Deposition date deposition_date2010-12-06
Structure title titleCrystal structure of (73-244)RIa:C holoenzyme of cAMP-dependent Protein kinase
Keywords keywordsKinase, RIa Holoenzyme, Tetrameric Protein Kinase A, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.27
Radius of gyration Rg (electron density) rg_electron24.17
Forward intensity I(0) i054600900.00
Molecular weight molecular_weight57223.0 kDa
Excluded volume excluded_volume71421 ų
Envelope volume envelope_volume85494 ų
Hydration-shell volume shell_volume29217 ų
Envelope diameter envelope_diameter88.9
Shell Rg shell_rg31.65
Envelope Rg envelope_rg24.44
Shape Rg shape_rg24.18
Total Rg total_rg24.97
Total atoms total_atoms4031
Residues n_residues501
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 dmax82.7
Rg (real space) rg_real25.18
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real5.4600e+07
I(0) uncertainty (real space) i0_real_error7.2880e+05
Rg (reciprocal space) rg_reciprocal25.21
I(0) (reciprocal space) i0_reciprocal54600000.0000
Solution quality estimate total_estimate0.8925
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary81.4
Skewness Skewness skewness0.238
Kurtosis Kurtosis kurtosis-0.410
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9876000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id3pvbA01
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_id3pvbA02
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_id3pvbB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls

8. Citations (1)

9. Files and Curves (10)