8utv

KIF1A[1-393] P305L mutant ADP bound in complex with a microtubule

Method: ELECTRON MICROSCOPY Dmax: 140.9 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 Chain E; UniProt 1–451 Not recorded Tubulin beta-2B chain × 1 (A0A287AGU7) Kinesin-like protein KIF1A × 1 (Q12756) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–451; UniProt 1–451 Author chain E; PDBConstruct 1–451; UniProt 1–451

Tubulin beta-2B chain

OrganismNot specified

UniProt A0A287AGU7

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 1–445 Not recorded Tubulin alpha-1B chain × 2 (Q2XVP4) Kinesin-like protein KIF1A × 1 (Q12756) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

98 other PDB entries and 98 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A287AGU7_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–445; UniProt 1–445

Kinesin-like protein KIF1A

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain K; UniProt 1–393 Fragment:residues 1-393 Mutation:P305L Tubulin alpha-1B chain × 2 (Q2XVP4) Tubulin beta-2B chain × 1 (A0A287AGU7) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 TA1 TAXOL × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 K; PDBConstruct 1–393; UniProt 1–393

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 8utv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8utv
Deposition date deposition_date2023-10-31
Structure title titleKIF1A[1-393] P305L mutant ADP bound in complex with a microtubule
Keywords keywordsKIF1A, kinesin, motility, microtubule, tubulin, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.56
Radius of gyration Rg (electron density) rg_electron41.36
Forward intensity I(0) i0570995000.00
Molecular weight molecular_weight190140.0 kDa
Excluded volume excluded_volume235270 ų
Envelope volume envelope_volume310400 ų
Hydration-shell volume shell_volume63425 ų
Envelope diameter envelope_diameter147.4
Shell Rg shell_rg45.86
Envelope Rg envelope_rg41.37
Shape Rg shape_rg41.37
Total Rg total_rg41.54
Total atoms total_atoms13337
Residues n_residues1679
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 dmax140.9
Rg (real space) rg_real41.65
Rg uncertainty (real space) rg_real_error1.28
I(0) (real space) i0_real5.7100e+08
I(0) uncertainty (real space) i0_real_error1.0280e+07
Rg (reciprocal space) rg_reciprocal41.57
I(0) (reciprocal space) i0_reciprocal570900000.0000
Solution quality estimate total_estimate0.8723
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.8
Skewness Skewness skewness0.396
Kurtosis Kurtosis kurtosis-0.392
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha196400000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.846; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.808

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)