5o09

BtubABC mini microtubule

Method: ELECTRON MICROSCOPY Dmax: 231.3 Å Quality: GOOD

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

Tubulin

Prosthecobacter dejongeii

UniProt Q8GCC5

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain 1A; UniProt 3–435 Chain 2A; UniProt 3–435 Chain 3A; UniProt 3–435 Chain 4A; UniProt 3–435 Chain 5A; UniProt 3–435 Chain 6A; UniProt 3–435 Chain 7A; UniProt 3–435 Chain 8A; UniProt 3–435 Not recorded Tubulin BtubB × 8 (Q8GCC1) Bacterial kinesin light chain × 8 (A8Y5U5) GDP GUANOSINE-5'-DIPHOSPHATE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8GCC5_9BACT
Isoform
PDB entities 1
Chains and sequence ranges Author chain 1A; PDBConstruct 1–433; UniProt 3–435 Author chain 2A; PDBConstruct 1–433; UniProt 3–435 Author chain 3A; PDBConstruct 1–433; UniProt 3–435 Author chain 4A; PDBConstruct 1–433; UniProt 3–435 Author chain 5A; PDBConstruct 1–433; UniProt 3–435 Author chain 6A; PDBConstruct 1–433; UniProt 3–435 Author chain 7A; PDBConstruct 1–433; UniProt 3–435 Author chain 8A; PDBConstruct 1–433; UniProt 3–435

Tubulin BtubB

Prosthecobacter dejongeii

UniProt Q8GCC1

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain 1B; UniProt 1–426 Chain 2B; UniProt 1–426 Chain 3B; UniProt 1–426 Chain 4B; UniProt 1–426 Chain 5B; UniProt 1–426 Chain 6B; UniProt 1–426 Chain 7B; UniProt 1–426 Chain 8B; UniProt 1–426 Not recorded Tubulin × 8 (Q8GCC5) Bacterial kinesin light chain × 8 (A8Y5U5) GDP GUANOSINE-5'-DIPHOSPHATE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8GCC1_9BACT
Isoform
PDB entities 2
Chains and sequence ranges Author chain 1B; PDBConstruct 1–426; UniProt 1–426 Author chain 2B; PDBConstruct 1–426; UniProt 1–426 Author chain 3B; PDBConstruct 1–426; UniProt 1–426 Author chain 4B; PDBConstruct 1–426; UniProt 1–426 Author chain 5B; PDBConstruct 1–426; UniProt 1–426 Author chain 6B; PDBConstruct 1–426; UniProt 1–426 Author chain 7B; PDBConstruct 1–426; UniProt 1–426 Author chain 8B; PDBConstruct 1–426; UniProt 1–426

Bacterial kinesin light chain

Prosthecobacter vanneervenii

UniProt A8Y5U5

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain 1C; UniProt 2–239 Chain 2C; UniProt 2–239 Chain 3C; UniProt 2–239 Chain 4C; UniProt 2–239 Chain 5C; UniProt 2–239 Chain 6C; UniProt 2–239 Chain 7C; UniProt 2–239 Chain 8C; UniProt 2–239 Not recorded Tubulin × 8 (Q8GCC5) Tubulin BtubB × 8 (Q8GCC1) GDP GUANOSINE-5'-DIPHOSPHATE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A8Y5U5_9BACT
Isoform
PDB entities 3
Chains and sequence ranges Author chain 1C; PDBConstruct 1–238; UniProt 2–239 Author chain 2C; PDBConstruct 1–238; UniProt 2–239 Author chain 3C; PDBConstruct 1–238; UniProt 2–239 Author chain 4C; PDBConstruct 1–238; UniProt 2–239 Author chain 5C; PDBConstruct 1–238; UniProt 2–239 Author chain 6C; PDBConstruct 1–238; UniProt 2–239 Author chain 7C; PDBConstruct 1–238; UniProt 2–239 Author chain 8C; PDBConstruct 1–238; UniProt 2–239

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 5o09

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5o09
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5o09
Deposition date deposition_date2017-05-16
Structure title titleBtubABC mini microtubule
Keywords keywordsbacterial cytoskeleton, microtubules, structural protein; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier69.65
Radius of gyration Rg (electron density) rg_electron69.09
Forward intensity I(0) i012885700000.00
Molecular weight molecular_weight958310.0 kDa
Excluded volume excluded_volume1197000 ų
Envelope volume envelope_volume1782100 ų
Hydration-shell volume shell_volume205870 ų
Envelope diameter envelope_diameter236.5
Shell Rg shell_rg77.20
Envelope Rg envelope_rg66.92
Shape Rg shape_rg69.10
Total Rg total_rg69.16
Total atoms total_atoms67424
Residues n_residues8648
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 dmax231.3
Rg (real space) rg_real69.40
Rg uncertainty (real space) rg_real_error2.83
I(0) (real space) i0_real1.2890e+10
I(0) uncertainty (real space) i0_real_error3.0210e+08
Rg (reciprocal space) rg_reciprocal70.45
I(0) (reciprocal space) i0_reciprocal12910000000.0000
Solution quality estimate total_estimate0.8460
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary84.1
Skewness Skewness skewness0.151
Kurtosis Kurtosis kurtosis-0.325
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha674400000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.774; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.920; Smooth: 0.750

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)