4hpt

Crystal structure of the catalytic subunit of cAMP-dependent protein kinase displaying complete phosphoryl transfer of AMP-PNP onto a substrate peptide

Method: X-RAY DIFFRACTION Dmax: 67.7 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 E; UniProt 2–351 Non-standard monomer:Yes (specific site not provided by mmCIF) cAMP-dependent protein kinase inhibitor alpha × 1 (P63248) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277.15 K;Protein buffer: 50 mM Bicine, 150 mM Ammonium Acetate, 10 mM DTT, ~7-10 mg/mL protein Well Solution: 1 mL of 2% MPD, 80 uL methanol added to the well immediately before sealing 8 uL drops of 1:1 protein:well were used., VAPOR DIFFUSION, HANGING DROP, temperature 277.15K, pH 8.0 Resolution 2.15 Å R-free 0.228

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 E; PDBConstruct 1–350; UniProt 2–351

cAMP-dependent protein kinase inhibitor alpha

OrganismNot specified

UniProt P63248

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 I; UniProt 6–25 Fragment:SP20 derived from PKI (unp residues 6-25) Mutation:N20A, A21S Non-standard monomer:Yes (specific site not provided by mmCIF) cAMP-dependent protein kinase catalytic subunit alpha × 1 (P05132) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277.15 K;Protein buffer: 50 mM Bicine, 150 mM Ammonium Acetate, 10 mM DTT, ~7-10 mg/mL protein Well Solution: 1 mL of 2% MPD, 80 uL methanol added to the well immediately before sealing 8 uL drops of 1:1 protein:well were used., VAPOR DIFFUSION, HANGING DROP, temperature 277.15K, pH 8.0 Resolution 2.15 Å R-free 0.228

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.

46 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IPKA_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; 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 4hpt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4hpt
Deposition date deposition_date2012-10-24
Structure title titleCrystal structure of the catalytic subunit of cAMP-dependent protein kinase displaying complete phosphoryl transfer of AMP-PNP onto a substrate peptide
Keywords keywordsProtein kinase, phosphotransferase, Regulatory subunits, PKI, magnesium, phosphorylation, transferase-transferase inhibitor complex; transferase/transferase inhibitor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.19
Radius of gyration Rg (electron density) rg_electron19.99
Forward intensity I(0) i028445000.00
Molecular weight molecular_weight41614.0 kDa
Excluded volume excluded_volume52349 ų
Envelope volume envelope_volume59626 ų
Hydration-shell volume shell_volume24097 ų
Envelope diameter envelope_diameter71.0
Shell Rg shell_rg27.33
Envelope Rg envelope_rg20.33
Shape Rg shape_rg19.96
Total Rg total_rg21.01
Total atoms total_atoms2937
Residues n_residues353
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 dmax67.7
Rg (real space) rg_real21.06
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real2.8440e+07
I(0) uncertainty (real space) i0_real_error3.5460e+05
Rg (reciprocal space) rg_reciprocal21.09
I(0) (reciprocal space) i0_reciprocal28450000.0000
Solution quality estimate total_estimate0.8863
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.9
Skewness Skewness skewness0.190
Kurtosis Kurtosis kurtosis-0.378
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7720000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.943

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4hptE01
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_id4hptE02
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)