4o22

Binary complex of metal-free PKAc with SP20.

Method: X-RAY DIFFRACTION Dmax: 68.7 Å Quality: REASONABLE

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 16–351 Fragment:Catalytic subunit, UNP residues 16-351 Non-standard monomer:Yes (specific site not provided by mmCIF) Phosphorylated peptide pSP20. × 1 (P61925) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;100 mM MES pH 6.5, 5 mM DTT, 15-20% PEG 3350., VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.70 Å R-free 0.219

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 7–342; UniProt 16–351

Phosphorylated peptide pSP20.

Homo sapiens

UniProt P61925

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 S; UniProt 6–25 Fragment:UNP residues 6-25 Mutation:N20A, A21S cAMP-dependent protein kinase catalytic subunit alpha. × 1 (P05132) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;100 mM MES pH 6.5, 5 mM DTT, 15-20% PEG 3350., VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.70 Å R-free 0.219

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.

90 other PDB entries and 100 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IPKA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain S; PDBConstruct 1–20; UniProt 6–25

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 4o22

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4o22
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4o22
Deposition date deposition_date2013-12-16
Structure title titleBinary complex of metal-free PKAc with SP20.
Keywords keywordsSer/Thr kinase, phosphoryl transfer, HYDROLASE-HYDROLASE INHIBITOR complex; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.61
Radius of gyration Rg (electron density) rg_electron20.25
Forward intensity I(0) i028106800.00
Molecular weight molecular_weight41765.0 kDa
Excluded volume excluded_volume52753 ų
Envelope volume envelope_volume60677 ų
Hydration-shell volume shell_volume24360 ų
Envelope diameter envelope_diameter71.0
Shell Rg shell_rg27.48
Envelope Rg envelope_rg20.46
Shape Rg shape_rg20.21
Total Rg total_rg21.33
Total atoms total_atoms2951
Residues n_residues356
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 dmax68.7
Rg (real space) rg_real21.46
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real2.8110e+07
I(0) uncertainty (real space) i0_real_error3.4960e+05
Rg (reciprocal space) rg_reciprocal21.49
I(0) (reciprocal space) i0_reciprocal28110000.0000
Solution quality estimate total_estimate0.7266
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.3
Skewness Skewness skewness0.163
Kurtosis Kurtosis kurtosis-0.403
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8016000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.870; Stabil: 1.000; Sysdev: 0.281; Positv: 1.000; Valcen: 0.994; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4o22a1
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
Domain ID domain_idd4o22a2
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_id4o22A01
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_id4o22A02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1

8. Citations (1)

9. Files and Curves (10)