2cpk

CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE

Method: X-RAY DIFFRACTION Dmax: 65.9 Å Quality: GOOD

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

cAMP-DEPENDENT PROTEIN KINASE, CATALYTIC SUBUNIT

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 1–350 Non-standard monomer:Yes (specific site not provided by mmCIF) PEPTIDE INHIBITOR 20-MER × 1 (P63248) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.70 Å

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 1–350

PEPTIDE INHIBITOR 20-MER

Mus musculus

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 5–24 Not recorded cAMP-DEPENDENT PROTEIN KINASE, CATALYTIC SUBUNIT × 1 (P05132) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.70 Å

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 5–24

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 2cpk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2cpk
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2cpk
Deposition date deposition_date1992-10-21
Structure title titleCRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE
Keywords keywordsTRANSFERASE(PHOSPHOTRANSFERASE); TRANSFERASE(PHOSPHOTRANSFERASE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.14
Radius of gyration Rg (electron density) rg_electron19.84
Forward intensity I(0) i025673200.00
Molecular weight molecular_weight39877.0 kDa
Excluded volume excluded_volume50285 ų
Envelope volume envelope_volume57124 ų
Hydration-shell volume shell_volume23519 ų
Envelope diameter envelope_diameter69.5
Shell Rg shell_rg26.82
Envelope Rg envelope_rg19.97
Shape Rg shape_rg19.82
Total Rg total_rg20.84
Total atoms total_atoms2822
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 dmax65.9
Rg (real space) rg_real20.99
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real2.5670e+07
I(0) uncertainty (real space) i0_real_error2.9140e+05
Rg (reciprocal space) rg_reciprocal21.02
I(0) (reciprocal space) i0_reciprocal25670000.0000
Solution quality estimate total_estimate0.8943
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.1
Skewness Skewness skewness0.153
Kurtosis Kurtosis kurtosis-0.397
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7234000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2cpke_
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_idd2cpki_
Class classj — Peptides
Fold Fold foldj.126 — cAMP-dependent protein kinase inhibitor
Superfamily Superfamily superfamilyj.126.1 — cAMP-dependent protein kinase inhibitor
Family Family familyj.126.1.1 — cAMP-dependent protein kinase inhibitor

CATH v4.4 (2 domains)

Domain ID domain_id2cpkE01
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_id2cpkE02
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 (3)

9. Files and Curves (10)