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1a06

CALMODULIN-DEPENDENT PROTEIN KINASE FROM RAT

Method: X-RAY DIFFRACTION Dmax: 67.5 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE

Rattus norvegicus

UniProt Q63450

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 1–333 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；pH 7.5 Resolution 2.50 Å R-free 0.313

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.

Other PDB Difference from Current Entry 1A06 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1MXE Structure of the Complex of Calmodulin with the Target Sequence of CaMKI Deposited 2002-10-02 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 294–318（25 aa） Fragment：Calmodulin Binding Domain
Not recorded CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；289 K；Cacodylate, Calcium chloride, MPD, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K
Resolution 1.70 Å R-free 0.229
1MXE Structure of the Complex of Calmodulin with the Target Sequence of CaMKI Deposited 2002-10-02 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 294–318（25 aa） Fragment：Calmodulin Binding Domain
Not recorded CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；289 K；Cacodylate, Calcium chloride, MPD, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K
Resolution 1.70 Å R-free 0.229
2L7L Solution structure of Ca2+/calmodulin complexed with a peptide representing the calmodulin-binding domain of calmodulin kinase I Deposited 2010-12-13 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 299–320（22 aa） Fragment：Calmodulin-binding residues 299-320
Not recorded CA CALCIUM ION × 4 SOLUTION NMR
NMR measurement conditions pH 6.8；303 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient
NMR measurement conditions pH 6.8；303 K；Ionic strength (raw mmCIF value) 0.3；Pressure ambient
NMR sample composition 0.95 mM [U-13C; U-15N] protein, 1.05 mM peptide, 4 mM CALCIUM ION, 0.5 mM DSS, 100 mM potassium chloride, 20 mM Bis-Tris, 0.03 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.66 mM [U-2H; U-15N] protein, 0.40 mM peptide, 20 mM Bis-Tris, 100 mM potassium chloride, 4 mM CALCIUM ION, 0.03 % sodium azide, 0.5 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.64 mM 1H/13C-methyl Met; U-2H; U-15N protein, 0.83 mM peptide, 20 mM Bis-Tris, 100 mM potassium chloride, 4 mM CALCIUM ION, 0.03 % sodium azide, 0.5 mM DSS, 100% D2O | 100% D2O
NMR sample composition 0.95 mM [U-13C; U-15N] protein, 1.05 mM peptide, 20 mM Bis-Tris, 300 mM potassium chloride, 4 mM CALCIUM ION, 0.03 % sodium azide, 0.5 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.95 mM [U-13C; U-15N] protein, 1.05 mM peptide, 20 mM Bis-Tris, 300 mM potassium chloride, 4 mM CALCIUM ION, 0.03 % sodium azide, 0.5 mM DSS, 16 w/v Pf1 phage, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided

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

View Construct and Data Evidence
UniProt name KCC1A_RAT
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–332； UniProt 1–333

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 1a06

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a06
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a06
Deposition date deposition_date1997-12-09
Structure title titleCALMODULIN-DEPENDENT PROTEIN KINASE FROM RAT
Keywords keywordsKINASE, SIGNAL TRANSDUCTION, CALCIUM/CALMODULIN; KINASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier21.25 Å
Radius of gyration Rg (electron density) rg_electron19.97 Å
Forward intensity I(0) i016211700.00
Molecular weight molecular_weight31408.0 kDa
Excluded volume excluded_volume39705 ų
Envelope volume envelope_volume46295 ų
Hydration-shell volume shell_volume19786 ų
Envelope diameter envelope_diameter69.1 Å
Shell Rg shell_rg26.04 Å
Envelope Rg envelope_rg20.12 Å
Shape Rg shape_rg19.98 Å
Total Rg total_rg20.82 Å
Total atoms total_atoms2221
Residues n_residues279
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax67.5 Å
Rg (real space) rg_real21.22 Å
Rg uncertainty (real space) rg_real_error0.33 Å
I(0) (real space) i0_real1.6210e+07
I(0) uncertainty (real space) i0_real_error2.1070e+05
Rg (reciprocal space) rg_reciprocal21.23 Å
I(0) (reciprocal space) i0_reciprocal16210000.0000
Solution quality estimate total_estimate0.9022
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.8 Å
Skewness Skewness skewness0.316
Kurtosis Kurtosis kurtosis-0.385
Angular range angular_range— – 0.3750 Å−1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha3245000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.998
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1a06a_
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_id1a06A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id1a06A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
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8. Citations (1)

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9. Files and Curves (10)