8x9p

HURP (428-534)-alpha-tubulin-beta-tubulin complex

Method: ELECTRON MICROSCOPY Dmax: 106.4 Å Quality: GOOD

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

Tubulin alpha chain

Bos taurus

UniProt A0A0M3KKT1

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 1–439 Not recorded Tubulin beta chain × 1 (P02554) Disks large-associated protein 5,Green fluorescent protein × 1 (Q15398,P42212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.54 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A0M3KKT1_TETTH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–439; UniProt 1–439

Tubulin beta chain

Bos taurus

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 B; UniProt 1–427 Not recorded Tubulin alpha chain × 1 (A0A0M3KKT1) Disks large-associated protein 5,Green fluorescent protein × 1 (Q15398,P42212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.54 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 B; PDBConstruct 1–427; UniProt 1–427

Disks large-associated protein 5,Green fluorescent protein

Homo sapiens

UniProt P42212

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 C; UniProt 2–217 Not recorded Tubulin alpha chain × 1 (A0A0M3KKT1) Tubulin beta chain × 1 (P02554) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.54 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 460–675; UniProt 2–217

Disks large-associated protein 5,Green fluorescent protein

Homo sapiens

UniProt Q15398

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 C; UniProt 199–619 Not recorded Tubulin alpha chain × 1 (A0A0M3KKT1) Tubulin beta chain × 1 (P02554) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.54 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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DLGP5_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 34–454; UniProt 199–619

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 8x9p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8x9p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8x9p
Deposition date deposition_date2023-11-30
Structure title titleHURP (428-534)-alpha-tubulin-beta-tubulin complex
Keywords keywordsHURP, tubulin, drug resistance, mitosis, CELL CYCLE; CELL CYCLE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.78
Radius of gyration Rg (electron density) rg_electron32.34
Forward intensity I(0) i0192084000.00
Molecular weight molecular_weight109150.0 kDa
Excluded volume excluded_volume135620 ų
Envelope volume envelope_volume166100 ų
Hydration-shell volume shell_volume43338 ų
Envelope diameter envelope_diameter116.2
Shell Rg shell_rg38.84
Envelope Rg envelope_rg32.38
Shape Rg shape_rg32.34
Total Rg total_rg32.81
Total atoms total_atoms7669
Residues n_residues973
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 dmax106.4
Rg (real space) rg_real32.89
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real1.9210e+08
I(0) uncertainty (real space) i0_real_error2.8200e+06
Rg (reciprocal space) rg_reciprocal32.85
I(0) (reciprocal space) i0_reciprocal192100000.0000
Solution quality estimate total_estimate0.8683
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.5
Skewness Skewness skewness0.463
Kurtosis Kurtosis kurtosis-0.259
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44420000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.861; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.716

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)