6ejn

The KLC2 TPR domain bound to the JIP3 leucine zipper domain

Method: X-RAY DIFFRACTION Dmax: 148.6 Å Quality: GOOD

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

Kinesin light chain 2

Mus musculus

UniProt Q91YS4

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 191–479 Chain B; UniProt 191–479 Not recorded C-Jun-amino-terminal kinase-interacting protein 3 × 2 (Q9ESN9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;298 K;20% PEG 3350 0.2 M NaCSN Resolution 3.20 Å R-free 0.210

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.

4 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q91YS4_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–291; UniProt 191–479 Author chain B; PDBConstruct 3–291; UniProt 191–479

C-Jun-amino-terminal kinase-interacting protein 3

Mus musculus

UniProt Q9ESN9

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 417–486 Chain D; UniProt 417–486 Not recorded Kinesin light chain 2 × 2 (Q91YS4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;298 K;20% PEG 3350 0.2 M NaCSN Resolution 3.20 Å R-free 0.210

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name JIP3_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 6–75; UniProt 417–486 Author chain D; PDBConstruct 6–75; UniProt 417–486

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 6ejn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ejn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ejn
Deposition date deposition_date2017-09-22
Structure title titleThe KLC2 TPR domain bound to the JIP3 leucine zipper domain
Keywords keywordskinesin JIP3 transport cargo molecular motor, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.29
Radius of gyration Rg (electron density) rg_electron42.43
Forward intensity I(0) i087129800.00
Molecular weight molecular_weight74086.0 kDa
Excluded volume excluded_volume92676 ų
Envelope volume envelope_volume142670 ų
Hydration-shell volume shell_volume32188 ų
Envelope diameter envelope_diameter152.2
Shell Rg shell_rg40.46
Envelope Rg envelope_rg41.38
Shape Rg shape_rg42.45
Total Rg total_rg42.21
Total atoms total_atoms5207
Residues n_residues659
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 dmax148.6
Rg (real space) rg_real42.74
Rg uncertainty (real space) rg_real_error2.40
I(0) (real space) i0_real8.7130e+07
I(0) uncertainty (real space) i0_real_error1.8100e+06
Rg (reciprocal space) rg_reciprocal42.30
I(0) (reciprocal space) i0_reciprocal87090000.0000
Solution quality estimate total_estimate0.7931
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.2
Skewness Skewness skewness0.484
Kurtosis Kurtosis kurtosis-0.441
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3228000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.698; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.606; Smooth: 0.606

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)