3j8x

High-resolution structure of no-nucleotide kinesin on microtubules

Method: ELECTRON MICROSCOPY Dmax: 111.1 Å Quality: GOOD

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

Kinesin-1 heavy chain

Homo sapiens

UniProt P33176

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 K; UniProt 1–349 Fragment:Truncated catalytic head domain (monomeric, UNP residues 1-349) Tubulin alpha-1B chain × 1 (Q2XVP4) Tubulin beta-2B chain × 1 (F2Z5B2) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:25 mM PIPES, 25 mM NaCl, 2 mM MgCl2, 1 mM EGTA;pH 6.8;25 mM PIPES, 25 mM NaCl, 2 mM MgCl2, 1 mM EGTA cryo-EM vitrification conditions:No glow discharge was applied. After sample application to grid, liquid was mostly 'wicked' away by edgewise application of filter paper. Subsequently, blotting and plunge freezing were performed with ~0.5 second delay after blotting but prior to plunging.;Cryogen ETHANE;No glow discharge was applied. After sample application to grid, liquid was mostly 'wicked' away by edgewise application of filter paper. Subsequently, blotting and plunge freezing were performed with ~0.5 second delay after blotting but prior to plunging into liquid ethane. Resolution 5.00 Å

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.

26 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KINH_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain K; PDBConstruct 1–349; UniProt 1–349

Tubulin alpha-1B chain

OrganismNot specified

UniProt Q2XVP4

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 1–451 Not recorded Kinesin-1 heavy chain × 1 (P33176) Tubulin beta-2B chain × 1 (F2Z5B2) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:25 mM PIPES, 25 mM NaCl, 2 mM MgCl2, 1 mM EGTA;pH 6.8;25 mM PIPES, 25 mM NaCl, 2 mM MgCl2, 1 mM EGTA cryo-EM vitrification conditions:No glow discharge was applied. After sample application to grid, liquid was mostly 'wicked' away by edgewise application of filter paper. Subsequently, blotting and plunge freezing were performed with ~0.5 second delay after blotting but prior to plunging.;Cryogen ETHANE;No glow discharge was applied. After sample application to grid, liquid was mostly 'wicked' away by edgewise application of filter paper. Subsequently, blotting and plunge freezing were performed with ~0.5 second delay after blotting but prior to plunging into liquid ethane. Resolution 5.00 Å

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.

230 other PDB entries and 243 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBA1B_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–451; UniProt 1–451

Tubulin beta-2B chain

OrganismNot specified

UniProt F2Z5B2

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 1–445 Not recorded Kinesin-1 heavy chain × 1 (P33176) Tubulin alpha-1B chain × 1 (Q2XVP4) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:25 mM PIPES, 25 mM NaCl, 2 mM MgCl2, 1 mM EGTA;pH 6.8;25 mM PIPES, 25 mM NaCl, 2 mM MgCl2, 1 mM EGTA cryo-EM vitrification conditions:No glow discharge was applied. After sample application to grid, liquid was mostly 'wicked' away by edgewise application of filter paper. Subsequently, blotting and plunge freezing were performed with ~0.5 second delay after blotting but prior to plunging.;Cryogen ETHANE;No glow discharge was applied. After sample application to grid, liquid was mostly 'wicked' away by edgewise application of filter paper. Subsequently, blotting and plunge freezing were performed with ~0.5 second delay after blotting but prior to plunging into liquid ethane. Resolution 5.00 Å

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.

9 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F2Z5B2_PIG
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–445; UniProt 1–445

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 3j8x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j8x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3j8x
Deposition date deposition_date2014-11-20
Structure title titleHigh-resolution structure of no-nucleotide kinesin on microtubules
Keywords keywordsmolecular motors, kinesin, myosin, microtubules, cytoskeletal motors, MOTOR PROTEIN-STRUCTURAL PROTEIN complex; MOTOR PROTEIN/STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.27
Radius of gyration Rg (electron density) rg_electron32.51
Forward intensity I(0) i0285961000.00
Molecular weight molecular_weight132420.0 kDa
Excluded volume excluded_volume164120 ų
Envelope volume envelope_volume204470 ų
Hydration-shell volume shell_volume50753 ų
Envelope diameter envelope_diameter118.3
Shell Rg shell_rg40.54
Envelope Rg envelope_rg32.90
Shape Rg shape_rg32.52
Total Rg total_rg33.07
Total atoms total_atoms9295
Residues n_residues1177
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 dmax111.1
Rg (real space) rg_real33.17
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real2.8600e+08
I(0) uncertainty (real space) i0_real_error4.3960e+06
Rg (reciprocal space) rg_reciprocal33.22
I(0) (reciprocal space) i0_reciprocal286000000.0000
Solution quality estimate total_estimate0.8855
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.3
Skewness Skewness skewness0.286
Kurtosis Kurtosis kurtosis-0.391
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha97910000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.847; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)