6kmh

The crystal structure of CASK/Mint1 complex

Method: X-RAY DIFFRACTION Dmax: 99.3 Å Quality: GOOD

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–319 Not recorded Amyloid-beta A4 precursor protein-binding family A member 1 × 1 (O35430) IOD IODIDE ION × 7 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.2M KI, 20% PEG 3350, pH 7.0 Resolution 2.40 Å R-free 0.224
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–319 Not recorded Amyloid-beta A4 precursor protein-binding family A member 1 × 1 (O35430) IOD IODIDE ION × 5 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.2M KI, 20% PEG 3350, pH 7.0 Resolution 2.40 Å R-free 0.224

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 44 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 Author chain B; PDBConstruct 7–325; UniProt 1–319

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 338–397 Not recorded Peripheral plasma membrane protein CASK × 1 (O14936) IOD IODIDE ION × 7 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.2M KI, 20% PEG 3350, pH 7.0 Resolution 2.40 Å R-free 0.224
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 338–397 Not recorded Peripheral plasma membrane protein CASK × 1 (O14936) IOD IODIDE ION × 5 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.2M KI, 20% PEG 3350, pH 7.0 Resolution 2.40 Å R-free 0.224

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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name APBA1_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 7–66; UniProt 338–397 Author chain D; 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 6kmh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6kmh
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6kmh
Deposition date deposition_date2019-07-31
Structure title titleThe crystal structure of CASK/Mint1 complex
Keywords keywordsCASK-CaMK domain, Mint1, CASK-Mint1 complex, hydrophobic interactions, 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_guinier29.62
Radius of gyration Rg (electron density) rg_electron28.94
Forward intensity I(0) i0118286000.00
Molecular weight molecular_weight84920.0 kDa
Excluded volume excluded_volume105550 ų
Envelope volume envelope_volume129930 ų
Hydration-shell volume shell_volume37282 ų
Envelope diameter envelope_diameter104.1
Shell Rg shell_rg36.40
Envelope Rg envelope_rg29.06
Shape Rg shape_rg28.99
Total Rg total_rg29.46
Total atoms total_atoms5875
Residues n_residues731
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 dmax99.3
Rg (real space) rg_real29.62
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real1.1830e+08
I(0) uncertainty (real space) i0_real_error1.6390e+06
Rg (reciprocal space) rg_reciprocal29.62
I(0) (reciprocal space) i0_reciprocal118300000.0000
Solution quality estimate total_estimate0.8810
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.1
Skewness Skewness skewness0.380
Kurtosis Kurtosis kurtosis-0.250
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha39040000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.929

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6kmha_
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.144.1.0 — automated matches
Domain ID domain_idd6kmhb_
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.144.1.0 — automated matches

8. Citations (1)

9. Files and Curves (10)