9di0

Cryo-EM structure of Kif18A bound to a microtubule

Method: ELECTRON MICROSCOPY Dmax: 108.8 Å Quality: GOOD

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

Kinesin-like protein KIF18A, Methylated-DNA--protein-cysteine methyltransferase chimera

Homo sapiens

UniProt E5BBQ0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 5–181 Not recorded Tubulin beta chain × 1 (P02554) Tubulin alpha-1B chain × 1 (Q2XVP4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 TA1 TAXOL × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name E5BBQ0_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 382–558; UniProt 5–181

Kinesin-like protein KIF18A, Methylated-DNA--protein-cysteine methyltransferase chimera

Homo sapiens

UniProt Q8NI77

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 2–374 Not recorded Tubulin beta chain × 1 (P02554) Tubulin alpha-1B chain × 1 (Q2XVP4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 TA1 TAXOL × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

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

View Construct and Data Evidence
UniProt name KI18A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–380; UniProt 2–374

Tubulin beta chain

OrganismNot specified

UniProt P02554

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain K; UniProt 1–445 Not recorded Kinesin-like protein KIF18A, Methylated-DNA--protein-cysteine methyltransferase chimera × 1 (Q8NI77,E5BBQ0) Tubulin alpha-1B chain × 1 (Q2XVP4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 TA1 TAXOL × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

137 other PDB entries and 159 assemblies. Open the comparison page and filter oligomeric states

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

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 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain L; UniProt 1–451 Not recorded Kinesin-like protein KIF18A, Methylated-DNA--protein-cysteine methyltransferase chimera × 1 (Q8NI77,E5BBQ0) Tubulin beta chain × 1 (P02554) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 TA1 TAXOL × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 3
Chains and sequence ranges Author chain L; PDBConstruct 1–451; UniProt 1–451

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 9di0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9di0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9di0
Deposition date deposition_date2024-09-04
最后修订 last_revision2025-07-16
Structure title titleCryo-EM structure of Kif18A bound to a microtubule
Keywords keywordsKif18A, Tubulin, K-fiber, mitosis, spindle, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.58
Radius of gyration Rg (electron density) rg_electron32.97
Forward intensity I(0) i0287987000.00
Molecular weight molecular_weight133390.0 kDa
Excluded volume excluded_volume165480 ų
Envelope volume envelope_volume207080 ų
Hydration-shell volume shell_volume50938 ų
Envelope diameter envelope_diameter116.0
Shell Rg shell_rg40.96
Envelope Rg envelope_rg33.24
Shape Rg shape_rg32.96
Total Rg total_rg33.56
Total atoms total_atoms9361
Residues n_residues1175
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 dmax108.8
Rg (real space) rg_real33.51
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real2.8800e+08
I(0) uncertainty (real space) i0_real_error4.1760e+06
Rg (reciprocal space) rg_reciprocal33.56
I(0) (reciprocal space) i0_reciprocal288000000.0000
Solution quality estimate total_estimate0.8955
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.4
Skewness Skewness skewness0.276
Kurtosis Kurtosis kurtosis-0.420
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha84300000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)