1bkx

A BINARY COMPLEX OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE AND ADENOSINE FURTHER DEFINES CONFORMATIONAL FLEXIBILITY

Method: X-RAY DIFFRACTION Dmax: 66.9 Å Quality: EXCELLENT

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

CAMP-DEPENDENT PROTEIN KINASE

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–350 Fragment:CATALYTIC SUBUNIT Non-standard monomer:Yes (specific site not provided by mmCIF) AMP ADENOSINE MONOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;THE RC.ADE BINARY COMPLEX CRYSTALS WERE GROWN AT 4 C BY THE HANGING-DROP VAPOR DIFFUSION METHOD. THE CRYSTALLIZATION DROPLET CONTAINED PROTEIN (0.5 MM), ADENOSINE (3 MM) AND 2-METHYL-2,4-PENTANEDIOL (MPD; 4%) IN 100 MM BICINE BUFFER AT PH 8.0. THE CRYSTALLIZATION WELL SOLUTION WAS MADE UP OF 15% MPD AND 100 MM AMMONIUM-SULFATE IN BICINE BUFFER (100 MM; PH 8.0). THE CRYSTALS GREW OVER THE COURSE OF 8-12 WEEKS TO A FINAL SIZE OF 0.2 X 0.3 X 0.5 MM3., vapor diffusion - hanging drop, temperature 277K Resolution 2.60 Å R-free 0.340

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 1–350; UniProt 1–350

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 1bkx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bkx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bkx
Deposition date deposition_date1997-07-01
Structure title titleA BINARY COMPLEX OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE AND ADENOSINE FURTHER DEFINES CONFORMATIONAL FLEXIBILITY
Keywords keywords;CONFORMATIONAL CHANGES, ELECTROSTATIC COMPLEMENTARITY, PHOSPHORYLATION, PROTEIN KINASE, TRANSFERASE, COMPLEX (PHOSPHOTRANSFERASE-ADENOSINE), PHOSPHOTRANSFERASE, COMPLEX (PHOSPHOTRANSFERASE-ADENOSINE) complex ;; COMPLEX (PHOSPHOTRANSFERASE/ADENOSINE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.58
Radius of gyration Rg (electron density) rg_electron20.26
Forward intensity I(0) i025442600.00
Molecular weight molecular_weight39887.0 kDa
Excluded volume excluded_volume50472 ų
Envelope volume envelope_volume58442 ų
Hydration-shell volume shell_volume23553 ų
Envelope diameter envelope_diameter69.7
Shell Rg shell_rg27.23
Envelope Rg envelope_rg20.50
Shape Rg shape_rg20.21
Total Rg total_rg21.32
Total atoms total_atoms2820
Residues n_residues337
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 dmax66.9
Rg (real space) rg_real21.44
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real2.5440e+07
I(0) uncertainty (real space) i0_real_error3.0910e+05
Rg (reciprocal space) rg_reciprocal21.47
I(0) (reciprocal space) i0_reciprocal25440000.0000
Solution quality estimate total_estimate0.9032
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.6
Skewness Skewness skewness0.172
Kurtosis Kurtosis kurtosis-0.430
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6019000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bkxa_
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

CATH v4.4 (2 domains)

Domain ID domain_id1bkxA01
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_id1bkxA02
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 (6)

9. Files and Curves (10)