3idc

Crystal structure of (102-265)RIIb:C holoenzyme of cAMP-dependent protein kinase

Method: X-RAY DIFFRACTION Dmax: 78.2 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–351 Fragment:Isoform 1 (C-alpha-1): UNP residues 2-351 Non-standard monomer:Yes (specific site not provided by mmCIF) cAMP-dependent protein kinase type II-beta regulatory subunit × 1 (P12369) MN MANGANESE (II) ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION UNDER OIL (VDUO);pH 7.5;298 K;8% PEG 3350, 40 mM Bis-Tris pH 7.5, 0.05 mM Na Acetate, VAPOR DIFFUSION UNDER OIL (VDUO), temperature 298K Resolution 2.70 Å R-free 0.319

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 1–350; UniProt 2–351

cAMP-dependent protein kinase type II-beta regulatory subunit

Rattus norvegicus

UniProt P12369

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 102–265 Fragment:UNP residues 102-265 cAMP-dependent protein kinase catalytic subunit alpha × 1 (P05132) MN MANGANESE (II) ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION UNDER OIL (VDUO);pH 7.5;298 K;8% PEG 3350, 40 mM Bis-Tris pH 7.5, 0.05 mM Na Acetate, VAPOR DIFFUSION UNDER OIL (VDUO), temperature 298K Resolution 2.70 Å R-free 0.319

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAP3_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–164; UniProt 102–265

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 3idc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3idc
Deposition date deposition_date2009-07-20
Structure title titleCrystal structure of (102-265)RIIb:C holoenzyme of cAMP-dependent protein kinase
Keywords keywords;PKA, cAMP, SPR, Affinity, Kinase, Linker, RII Holoenzyme, Alternative splicing, ATP-binding, Cytoplasm, Lipoprotein, Myristate, Nucleotide-binding, Nucleus, Phosphoprotein, Serine/threonine-protein kinase, Transferase, Acetylation, cAMP-binding ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.84
Radius of gyration Rg (electron density) rg_electron23.56
Forward intensity I(0) i052900500.00
Molecular weight molecular_weight55385.0 kDa
Excluded volume excluded_volume68693 ų
Envelope volume envelope_volume83845 ų
Hydration-shell volume shell_volume29211 ų
Envelope diameter envelope_diameter80.6
Shell Rg shell_rg31.00
Envelope Rg envelope_rg23.80
Shape Rg shape_rg23.60
Total Rg total_rg24.27
Total atoms total_atoms3905
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 dmax78.2
Rg (real space) rg_real24.72
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real5.2900e+07
I(0) uncertainty (real space) i0_real_error7.5090e+05
Rg (reciprocal space) rg_reciprocal24.75
I(0) (reciprocal space) i0_reciprocal52900000.0000
Solution quality estimate total_estimate0.9039
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.8
Skewness Skewness skewness0.211
Kurtosis Kurtosis kurtosis-0.452
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10280000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3idca_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit

CATH v4.4 (3 domains)

Domain ID domain_id3idcA01
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_id3idcA02
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_id3idcB01
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)