8ixd

GMPCPP-Alpha1C/Beta2A-microtubule decorated with kinesin non-seam region

Method: ELECTRON MICROSCOPY Dmax: 232.3 Å Quality: EXCELLENT

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

Tubulin alpha-1C chain

Mus musculus

UniProt P68373

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain A; UniProt 1–449 Chain B; UniProt 1–449 Chain C; UniProt 1–449 Chain D; UniProt 1–449 Chain E; UniProt 1–449 Chain F; UniProt 1–449 Chain G; UniProt 1–449 Chain H; UniProt 1–449 Chain I; UniProt 1–449 Not recorded Tubulin beta-2A chain × 9 (Q7TMM9) Kinesin-1 heavy chain × 9 (P33176) GTP GUANOSINE-5'-TRIPHOSPHATE × 9 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBA1C_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–455; UniProt 1–449 Author chain B; PDBConstruct 1–455; UniProt 1–449 Author chain C; PDBConstruct 1–455; UniProt 1–449 Author chain D; PDBConstruct 1–455; UniProt 1–449 Author chain E; PDBConstruct 1–455; UniProt 1–449 Author chain F; PDBConstruct 1–455; UniProt 1–449 Author chain G; PDBConstruct 1–455; UniProt 1–449 Author chain H; PDBConstruct 1–455; UniProt 1–449 Author chain I; PDBConstruct 1–455; UniProt 1–449

Tubulin beta-2A chain

Mus musculus

UniProt Q7TMM9

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain J; UniProt 1–445 Chain K; UniProt 1–445 Chain L; UniProt 1–445 Chain M; UniProt 1–445 Chain N; UniProt 1–445 Chain O; UniProt 1–445 Chain P; UniProt 1–445 Chain Q; UniProt 1–445 Chain R; UniProt 1–445 Not recorded Tubulin alpha-1C chain × 9 (P68373) Kinesin-1 heavy chain × 9 (P33176) GTP GUANOSINE-5'-TRIPHOSPHATE × 9 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBB2A_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain J; PDBConstruct 1–445; UniProt 1–445 Author chain K; PDBConstruct 1–445; UniProt 1–445 Author chain L; PDBConstruct 1–445; UniProt 1–445 Author chain M; PDBConstruct 1–445; UniProt 1–445 Author chain N; PDBConstruct 1–445; UniProt 1–445 Author chain O; PDBConstruct 1–445; UniProt 1–445 Author chain P; PDBConstruct 1–445; UniProt 1–445 Author chain Q; PDBConstruct 1–445; UniProt 1–445 Author chain R; PDBConstruct 1–445; UniProt 1–445

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain S; UniProt 1–349 Chain T; UniProt 1–349 Chain U; UniProt 1–349 Chain V; UniProt 1–349 Chain W; UniProt 1–349 Chain X; UniProt 1–349 Chain Y; UniProt 1–349 Chain Z; UniProt 1–349 Chain a; UniProt 1–349 Not recorded Tubulin alpha-1C chain × 9 (P68373) Tubulin beta-2A chain × 9 (Q7TMM9) GTP GUANOSINE-5'-TRIPHOSPHATE × 9 G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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 3
Chains and sequence ranges Author chain S; PDBConstruct 24–372; UniProt 1–349 Author chain T; PDBConstruct 24–372; UniProt 1–349 Author chain U; PDBConstruct 24–372; UniProt 1–349 Author chain V; PDBConstruct 24–372; UniProt 1–349 Author chain W; PDBConstruct 24–372; UniProt 1–349 Author chain X; PDBConstruct 24–372; UniProt 1–349 Author chain Y; PDBConstruct 24–372; UniProt 1–349 Author chain Z; PDBConstruct 24–372; UniProt 1–349 Author chain a; PDBConstruct 24–372; UniProt 1–349

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 8ixd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8ixd
Deposition date deposition_date2023-03-31
Structure title titleGMPCPP-Alpha1C/Beta2A-microtubule decorated with kinesin non-seam region
Keywords keywordsmicrotubule, tubulin isotype, cryo-EM structure, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier87.69
Radius of gyration Rg (electron density) rg_electron87.97
Forward intensity I(0) i021080000000.00
Molecular weight molecular_weight1199500.0 kDa
Excluded volume excluded_volume1484600 ų
Envelope volume envelope_volume2249800 ų
Hydration-shell volume shell_volume214310 ų
Envelope diameter envelope_diameter318.2
Shell Rg shell_rg80.55
Envelope Rg envelope_rg85.85
Shape Rg shape_rg87.97
Total Rg total_rg87.91
Total atoms total_atoms84096
Residues n_residues10602
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 dmax232.3
Rg (real space) rg_real84.16
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real2.0140e+10
I(0) uncertainty (real space) i0_real_error4.1810e+08
Rg (reciprocal space) rg_reciprocal86.38
I(0) (reciprocal space) i0_reciprocal20990000000.0000
Solution quality estimate total_estimate0.9117
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary90.3
Skewness Skewness skewness0.259
Kurtosis Kurtosis kurtosis-0.639
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha1.0130
Highest regularization parameter α highest_alpha750900000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 1.000; Stabil: 0.966; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.002

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)