4uxs

Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins

Method: ELECTRON MICROSCOPY Dmax: 108.4 Å Quality: GOOD

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

TUBULIN ALPHA-1B CHAIN

OrganismNot specified

UniProt P81947

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 TUBULIN BETA-2B CHAIN × 1 (Q6B856) KINESIN-3 MOTOR DOMAIN × 1 (Q12756) ZN ZINC ION × 1 MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1 ELECTRON MICROSCOPY cryo-EM buffer:20MM PIPES, 2MM MGCL2, 1MM EGTA, 2MM DTT, 2MM ADP;pH 6.8;20MM PIPES, 2MM MGCL2, 1MM EGTA, 2MM DTT, 2MM ADP cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 7.00 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.

249 other PDB entries and 251 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBA1B_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–451; UniProt 1–451

TUBULIN BETA-2B CHAIN

OrganismNot specified

UniProt Q6B856

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 TUBULIN ALPHA-1B CHAIN × 1 (P81947) KINESIN-3 MOTOR DOMAIN × 1 (Q12756) ZN ZINC ION × 1 MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1 ELECTRON MICROSCOPY cryo-EM buffer:20MM PIPES, 2MM MGCL2, 1MM EGTA, 2MM DTT, 2MM ADP;pH 6.8;20MM PIPES, 2MM MGCL2, 1MM EGTA, 2MM DTT, 2MM ADP cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 7.00 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.

273 other PDB entries and 275 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBB2B_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–445; UniProt 1–445

KINESIN-3 MOTOR DOMAIN

HOMO SAPIENS

UniProt Q12756

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 1–361 Not recorded TUBULIN ALPHA-1B CHAIN × 1 (P81947) TUBULIN BETA-2B CHAIN × 1 (Q6B856) ZN ZINC ION × 1 MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1 ELECTRON MICROSCOPY cryo-EM buffer:20MM PIPES, 2MM MGCL2, 1MM EGTA, 2MM DTT, 2MM ADP;pH 6.8;20MM PIPES, 2MM MGCL2, 1MM EGTA, 2MM DTT, 2MM ADP cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 7.00 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.

20 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KIF1A_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–367; UniProt 1–361

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 4uxs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4uxs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4uxs
Deposition date deposition_date2014-08-27
Structure title titleConserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins
Keywords keywordsTRANSPORT PROTEIN, KINESIN, MICROTUBULE, CRYO-EM; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.36
Radius of gyration Rg (electron density) rg_electron32.87
Forward intensity I(0) i0286930000.00
Molecular weight molecular_weight133620.0 kDa
Excluded volume excluded_volume162080 ų
Envelope volume envelope_volume138040 ų
Hydration-shell volume shell_volume37310 ų
Envelope diameter envelope_diameter113.2
Shell Rg shell_rg37.41
Envelope Rg envelope_rg31.30
Shape Rg shape_rg32.62
Total Rg total_rg33.14
Total atoms total_atoms124
Residues n_residues
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 dmax108.4
Rg (real space) rg_real33.30
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real2.8690e+08
I(0) uncertainty (real space) i0_real_error3.8840e+06
Rg (reciprocal space) rg_reciprocal33.34
I(0) (reciprocal space) i0_reciprocal286900000.0000
Solution quality estimate total_estimate0.8991
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.9
Skewness Skewness skewness0.279
Kurtosis Kurtosis kurtosis-0.421
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha63580000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.899; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)