4x6r

An Isoform-specific Myristylation Switch Targets RIIb PKA Holoenzymes to Membranes

Method: X-RAY DIFFRACTION Dmax: 96.6 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 2–351 Mutation:K7C Non-standard monomer:Yes (specific site not provided by mmCIF) cAMP-dependent protein kinase type I-alpha regulatory subunit × 1 (P00514) SO4 SULFATE ION × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 1 GOL GLYCEROL × 2 MYR MYRISTIC ACID × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:BATCH MODE;298 K;Crystallization of RIb(91-379,R333K): myrC(K7C) heterodimer :RC heterodimer that was concentrated to 14 mg/mL and screened against different ammonium sulfate concentrations ranging from 0.8-2.5 M in 0.1 M sodium citrate buffer and also varying the pH from 5.0-6.0 using the hanging drop vapor diffusion method. The crystal used for structure determination was obtained from a 4 uL drop containing 1:1 protein to well solution with the well solution containing 1.6 M ammonium sulfate and 0.1 M sodium citrate at pH 5.5 Resolution 2.40 Å R-free 0.234

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 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 91–380 Mutation:R333K cAMP-dependent protein kinase catalytic subunit alpha × 1 (P05132) SO4 SULFATE ION × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 1 GOL GLYCEROL × 2 MYR MYRISTIC ACID × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:BATCH MODE;298 K;Crystallization of RIb(91-379,R333K): myrC(K7C) heterodimer :RC heterodimer that was concentrated to 14 mg/mL and screened against different ammonium sulfate concentrations ranging from 0.8-2.5 M in 0.1 M sodium citrate buffer and also varying the pH from 5.0-6.0 using the hanging drop vapor diffusion method. The crystal used for structure determination was obtained from a 4 uL drop containing 1:1 protein to well solution with the well solution containing 1.6 M ammonium sulfate and 0.1 M sodium citrate at pH 5.5 Resolution 2.40 Å R-free 0.234

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 1–290; UniProt 91–380

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 4x6r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4x6r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4x6r
Deposition date deposition_date2014-12-09
Structure title titleAn Isoform-specific Myristylation Switch Targets RIIb PKA Holoenzymes to Membranes
Keywords keywordsPKA, membrane binding, molecular switch, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.82
Radius of gyration Rg (electron density) rg_electron27.72
Forward intensity I(0) i090157100.00
Molecular weight molecular_weight74601.0 kDa
Excluded volume excluded_volume93393 ų
Envelope volume envelope_volume115830 ų
Hydration-shell volume shell_volume34861 ų
Envelope diameter envelope_diameter101.3
Shell Rg shell_rg34.86
Envelope Rg envelope_rg28.12
Shape Rg shape_rg27.70
Total Rg total_rg28.49
Total atoms total_atoms5246
Residues n_residues637
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 dmax96.6
Rg (real space) rg_real28.78
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real9.0160e+07
I(0) uncertainty (real space) i0_real_error1.4310e+06
Rg (reciprocal space) rg_reciprocal28.80
I(0) (reciprocal space) i0_reciprocal90160000.0000
Solution quality estimate total_estimate0.8860
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.4
Skewness Skewness skewness0.327
Kurtosis Kurtosis kurtosis-0.276
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17590000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.974

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4x6ra_
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 (4 domains)

Domain ID domain_id4x6rA01
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_id4x6rA02
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_id4x6rB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls
Domain ID domain_id4x6rB02
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)