8yy5

Kinesin-14 with AlF3 bound to 14 PF Microtubule

Method: ELECTRON MICROSCOPY Dmax: 137.9 Å Quality: GOOD

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

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–451 Not recorded Tubulin beta chain × 1 (Q767L7) Protein claret segregational × 2 (P20480) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ALF TETRAFLUOROALUMINATE ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8;100 mM PIPES pH 6.8, 1 mM MgCl2, 1 mM EGTA, 1 mM GTP, 2 mM ADP, 2 mM AlCl3, and 8 mM NaF cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.99 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–451; UniProt 1–451

Tubulin beta chain

OrganismNot specified

UniProt Q767L7

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 B; UniProt 1–444 Not recorded Tubulin alpha-1B chain × 1 (Q2XVP4) Protein claret segregational × 2 (P20480) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ALF TETRAFLUOROALUMINATE ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8;100 mM PIPES pH 6.8, 1 mM MgCl2, 1 mM EGTA, 1 mM GTP, 2 mM ADP, 2 mM AlCl3, and 8 mM NaF cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.99 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBB5_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–444; UniProt 1–444

Protein claret segregational

Drosophila melanogaster

UniProt P20480

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 292–700 Chain D; UniProt 292–700 Mutation:E292M, Y485K, N697S Tubulin alpha-1B chain × 1 (Q2XVP4) Tubulin beta chain × 1 (Q767L7) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ALF TETRAFLUOROALUMINATE ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8;100 mM PIPES pH 6.8, 1 mM MgCl2, 1 mM EGTA, 1 mM GTP, 2 mM ADP, 2 mM AlCl3, and 8 mM NaF cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.99 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.

15 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NCD_DROME
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–409; UniProt 292–700 Author chain D; PDBConstruct 1–409; UniProt 292–700

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 8yy5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8yy5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8yy5
Deposition date deposition_date2024-04-03
Structure title titleKinesin-14 with AlF3 bound to 14 PF Microtubule
Keywords keywords;Kinesin Motor Proteins, Force Production, Power Stroke Fluctuations, Motor Spring-like Element, Reversed Motility, Mechanochemical Coupling, Mechanical States, CELL CYCLE ;; CELL CYCLE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.74
Radius of gyration Rg (electron density) rg_electron40.50
Forward intensity I(0) i0488973000.00
Molecular weight molecular_weight175690.0 kDa
Excluded volume excluded_volume217580 ų
Envelope volume envelope_volume279330 ų
Hydration-shell volume shell_volume57889 ų
Envelope diameter envelope_diameter139.8
Shell Rg shell_rg45.34
Envelope Rg envelope_rg40.39
Shape Rg shape_rg40.50
Total Rg total_rg40.74
Total atoms total_atoms12315
Residues n_residues1545
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 dmax137.9
Rg (real space) rg_real40.82
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real4.8900e+08
I(0) uncertainty (real space) i0_real_error1.0060e+07
Rg (reciprocal space) rg_reciprocal40.74
I(0) (reciprocal space) i0_reciprocal488900000.0000
Solution quality estimate total_estimate0.8752
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.4
Skewness Skewness skewness0.375
Kurtosis Kurtosis kurtosis-0.471
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha121900000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.919; Smooth: 0.881

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (2)

9. Files and Curves (10)