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6f9i

Crystal structure of KLC2 bound to the second tryptophan-acidic motif peptide from calsyntenin-1

Method: X-RAY DIFFRACTION Dmax: 137.8 Å Quality: REASONABLE
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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 191–481 Chain B； UniProt 191–481 Not recorded Calsyntenin-1 × 2 （Q9EPL2） X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；298 K；0.893 M sodium potassium tartrate, 0.2 M NaCl, 0.1 M imidazole pH 8.0 Resolution 3.99 Å R-free 0.273

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 6F9I Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3ZFW Crystal structure of the TPR domain of kinesin light chain 2 in complex with a tryptophan-acidic cargo peptide Deposited 2012-12-12 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 218–480（263 aa） Fragment：TPR DOMAIN, RESIDUES 218-477
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；0.10 M MES PH 6.5, 0.2 L-PROLINE, 7% PGA
Resolution 2.90 Å R-free 0.244
3ZFW Crystal structure of the TPR domain of kinesin light chain 2 in complex with a tryptophan-acidic cargo peptide Deposited 2012-12-12 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 218–480（263 aa） Fragment：TPR DOMAIN, RESIDUES 218-477
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；0.10 M MES PH 6.5, 0.2 L-PROLINE, 7% PGA
Resolution 2.90 Å R-free 0.244
5FJY Crystal structure of mouse kinesin light chain 2 (residues 161-480) Deposited 2015-10-14 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 161–480（320 aa） Fragment：TPR DOMAIN WITH N-TERMINAL EXTENSION
Chain B 161–480（320 aa） Fragment：TPR DOMAIN WITH N-TERMINAL EXTENSION
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；8% (W/V) PGA-LM 0.3 M NA-MALONATE 0.1 M NA-CACODYLATE PH 6.5
Resolution 4.00 Å R-free 0.261
5FJY Crystal structure of mouse kinesin light chain 2 (residues 161-480) Deposited 2015-10-14 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 161–480（320 aa） Fragment：TPR DOMAIN WITH N-TERMINAL EXTENSION
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；8% (W/V) PGA-LM 0.3 M NA-MALONATE 0.1 M NA-CACODYLATE PH 6.5
Resolution 4.00 Å R-free 0.261
5OJF Crystal Structure of KLC2-TPR domain (fragment [A1-B6] Deposited 2017-07-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 190–484（295 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；12 % PEG 3350, 0.5 M Phos. pH 7.5 Glycerol 25 %
Resolution 3.40 Å R-free 0.264
5OJF Crystal Structure of KLC2-TPR domain (fragment [A1-B6] Deposited 2017-07-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 190–484（295 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；12 % PEG 3350, 0.5 M Phos. pH 7.5 Glycerol 25 %
Resolution 3.40 Å R-free 0.264
5OJF Crystal Structure of KLC2-TPR domain (fragment [A1-B6] Deposited 2017-07-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 190–484（295 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；12 % PEG 3350, 0.5 M Phos. pH 7.5 Glycerol 25 %
Resolution 3.40 Å R-free 0.264
6EJN The KLC2 TPR domain bound to the JIP3 leucine zipper domain Deposited 2017-09-22 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 191–479（289 aa）
Chain B 191–479（289 aa）
Not recorded No recorded non-water small molecule 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

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 3–293； UniProt 191–481 Author chain B； PDBConstruct 3–293； UniProt 191–481

Calsyntenin-1

OrganismNot specified

UniProt Q9EPL2

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 965–979 Chain X； UniProt 965–979 Not recorded Kinesin light chain 2 × 2 （Q91YS4） X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；298 K；0.893 M sodium potassium tartrate, 0.2 M NaCl, 0.1 M imidazole pH 8.0 Resolution 3.99 Å R-free 0.273

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 CSTN1_MOUSE
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C； PDBConstruct 1–15； UniProt 965–979 Author chain X； PDBConstruct 1–15； UniProt 965–979

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 6f9i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6f9i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6f9i
Deposition date deposition_date2017-12-14
Structure title titleCrystal structure of KLC2 bound to the second tryptophan-acidic motif peptide from calsyntenin-1
Keywords keywordskinesin, cargo, activation, transport, MOTOR PROTEIN; MOTOR PROTEIN
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_guinier39.72 Å
Radius of gyration Rg (electron density) rg_electron40.11 Å
Forward intensity I(0) i061657800.00
Molecular weight molecular_weight61497.0 kDa
Excluded volume excluded_volume76579 ų
Envelope volume envelope_volume114490 ų
Hydration-shell volume shell_volume27419 ų
Envelope diameter envelope_diameter139.6 Å
Shell Rg shell_rg38.99 Å
Envelope Rg envelope_rg39.38 Å
Shape Rg shape_rg40.14 Å
Total Rg total_rg39.94 Å
Total atoms total_atoms8650
Residues n_residues544
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 dmax137.8 Å
Rg (real space) rg_real40.47 Å
Rg uncertainty (real space) rg_real_error1.70 Å
I(0) (real space) i0_real6.1660e+07
I(0) uncertainty (real space) i0_real_error1.1560e+06
Rg (reciprocal space) rg_reciprocal40.02 Å
I(0) (reciprocal space) i0_reciprocal61630000.0000
Solution quality estimate total_estimate0.7197
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1 Å
Skewness Skewness skewness0.486
Kurtosis Kurtosis kurtosis-0.615
Angular range angular_range— – 0.2000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2681000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.544; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.262; Smooth: 0.457
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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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8. Citations (1)

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9. Files and Curves (10)