2izx

Molecular Basis of AKAP Specificity for PKA Regulatory Subunits

Method: X-RAY DIFFRACTION Dmax: 43.6 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

CAMP-DEPENDENT PROTEIN KINASE TYPE II-ALPHA REGULATORY SUBUNIT

HOMO SAPIENS

UniProt P13861

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 3–43 Chain B; UniProt 3–43 Fragment:3-43 AKAP-IS × 1 DTD DITHIANE DIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;1 M TRI-SODIUM CITRATE, 0.1 M TRIS-HCL PH 7.5 Resolution 1.30 Å R-free 0.194

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.

7 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAP2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–41; UniProt 3–43 Author chain B; PDBConstruct 1–41; UniProt 3–43

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 2izx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2izx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2izx
Deposition date deposition_date2006-07-27
Structure title titleMolecular Basis of AKAP Specificity for PKA Regulatory Subunits
Keywords keywordsCAMP-BINDING, PHOSPHORYLATION, NUCLEOTIDE-BINDING, PKA, CAMP, AKAP, ANCHOR, KINASE, ACETYLATION, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.29
Radius of gyration Rg (electron density) rg_electron12.71
Forward intensity I(0) i02601120.00
Molecular weight molecular_weight11596.0 kDa
Excluded volume excluded_volume14736 ų
Envelope volume envelope_volume15946 ų
Hydration-shell volume shell_volume10693 ų
Envelope diameter envelope_diameter42.0
Shell Rg shell_rg18.38
Envelope Rg envelope_rg13.00
Shape Rg shape_rg12.68
Total Rg total_rg14.11
Total atoms total_atoms816
Residues n_residues98
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 dmax43.6
Rg (real space) rg_real14.17
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real2.6010e+06
I(0) uncertainty (real space) i0_real_error3.1680e+04
Rg (reciprocal space) rg_reciprocal14.18
I(0) (reciprocal space) i0_reciprocal2601000.0000
Solution quality estimate total_estimate0.8944
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.5
Skewness Skewness skewness0.013
Kurtosis Kurtosis kurtosis-0.412
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha440000.0000
Real-space data points n_real_points80
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: 0.979; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2izxa_
Class classa — All alpha proteins
Fold Fold folda.31 — Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit
Superfamily Superfamily superfamilya.31.1 — Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit
Family Family familya.31.1.1 — Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit
Domain ID domain_idd2izxb_
Class classa — All alpha proteins
Fold Fold folda.31 — Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit
Superfamily Superfamily superfamilya.31.1 — Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit
Family Family familya.31.1.1 — Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit

CATH v4.4 (1 domains)

Domain ID domain_id2izxB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology890 — cAMP-dependent Protein Kinase, Chain A
Homologous superfamily homologous superfamily10 — cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain

8. Citations (1)

9. Files and Curves (10)