9m6g

the crystal structure of the Ca2+/CaM-CASK-CaMK-Mint1-CID complex

Method: X-RAY DIFFRACTION Dmax: 68.0 Å Quality: EXCELLENT

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

Peripheral plasma membrane protein CASK

Homo sapiens

UniProt O14936

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–319 Not recorded Calmodulin-1 × 1 (P0DP29) Amyloid-beta A4 precursor protein-binding family A member 1 × 1 (O35430) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MLI MALONATE ION × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;289 K;0.1 M Sodium malonate, pH 5.0, 12% (v/v) PEG 3350 Resolution 1.70 Å R-free 0.187

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.

21 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSKP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–325; UniProt 1–319

Calmodulin-1

Rattus norvegicus

UniProt P0DP29

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–149 Not recorded Peripheral plasma membrane protein CASK × 1 (O14936) Amyloid-beta A4 precursor protein-binding family A member 1 × 1 (O35430) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MLI MALONATE ION × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;289 K;0.1 M Sodium malonate, pH 5.0, 12% (v/v) PEG 3350 Resolution 1.70 Å R-free 0.187

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.

32 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM1_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–153; UniProt 1–149

Amyloid-beta A4 precursor protein-binding family A member 1

Rattus norvegicus

UniProt O35430

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 338–397 Not recorded Peripheral plasma membrane protein CASK × 1 (O14936) Calmodulin-1 × 1 (P0DP29) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MLI MALONATE ION × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;289 K;0.1 M Sodium malonate, pH 5.0, 12% (v/v) PEG 3350 Resolution 1.70 Å R-free 0.187

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.

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name APBA1_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 7–66; UniProt 338–397

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 9m6g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9m6g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9m6g
Deposition date deposition_date2025-03-07
Structure title titlethe crystal structure of the Ca2+/CaM-CASK-CaMK-Mint1-CID complex
Keywords keywordsCa2+/CaM, CASK-CaMK, Mint1-CID, AMPPNP, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.26
Radius of gyration Rg (electron density) rg_electron21.00
Forward intensity I(0) i033322000.00
Molecular weight molecular_weight44139.0 kDa
Excluded volume excluded_volume55134 ų
Envelope volume envelope_volume65104 ų
Hydration-shell volume shell_volume25313 ų
Envelope diameter envelope_diameter67.6
Shell Rg shell_rg28.15
Envelope Rg envelope_rg21.12
Shape Rg shape_rg21.02
Total Rg total_rg21.83
Total atoms total_atoms3092
Residues n_residues382
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 dmax68.0
Rg (real space) rg_real22.11
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real3.3320e+07
I(0) uncertainty (real space) i0_real_error3.8460e+05
Rg (reciprocal space) rg_reciprocal22.14
I(0) (reciprocal space) i0_reciprocal33320000.0000
Solution quality estimate total_estimate0.9067
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.8
Skewness Skewness skewness0.078
Kurtosis Kurtosis kurtosis-0.557
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7245000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.934; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)