1r2a

THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY SOLUTION NMR

Method: SOLUTION NMR Dmax: 66.8 Å Quality: REASONABLE

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

PROTEIN (CAMP-DEPENDENT PROTEIN KINASE TYPE II REGULATORY SUBUNIT)

Mus musculus

UniProt P12367

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–44 Chain B; UniProt 1–44 Fragment:DIMERIZATION-ANCHORING DOMAIN No other associated polymer SOLUTION NMR NMR measurement conditions:pH 4;298 K;Ionic strength (raw mmCIF value) 0.012 mM;Pressure 1 Resolution not provided

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAP2_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–46; UniProt 1–44 Author chain B; PDBConstruct 2–46; UniProt 1–44

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 1r2a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1r2a
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1r2a
Deposition date deposition_date1998-12-07
Structure title titleTHE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY SOLUTION NMR
Keywords keywordsREGULATORY SUBUNIT, ANCHORING, FOUR-HELIX BUNDLE, TRANSFERASE; TRANSFERASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.32
Radius of gyration Rg (electron density) rg_electron15.25
Forward intensity I(0) i0462209000.00
Molecular weight molecular_weight183270.0 kDa
Excluded volume excluded_volume230520 ų
Envelope volume envelope_volume43611 ų
Hydration-shell volume shell_volume18497 ų
Envelope diameter envelope_diameter73.1
Shell Rg shell_rg26.29
Envelope Rg envelope_rg21.29
Shape Rg shape_rg15.16
Total Rg total_rg15.88
Total atoms total_atoms25942
Residues n_residues1564
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 dmax66.8
Rg (real space) rg_real16.39
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real4.6220e+08
I(0) uncertainty (real space) i0_real_error5.9650e+06
Rg (reciprocal space) rg_reciprocal16.38
I(0) (reciprocal space) i0_reciprocal462200000.0000
Solution quality estimate total_estimate0.7135
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.1
Skewness Skewness skewness0.470
Kurtosis Kurtosis kurtosis-0.001
Angular range angular_range— – 0.4900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha324900.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.203; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.662; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1r2aa1
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_idd1r2aa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1r2ab1
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_idd1r2ab2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id1r2aA00
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
Domain ID domain_id1r2aB00
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 (2)

9. Files and Curves (10)