9cmm

Two protofilament structure of alpha1B and betaI/IVb microtubule bound to GMPCPP

Method: ELECTRON MICROSCOPY Dmax: 204.3 Å Quality: GOOD

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

Tubulin beta chain

OrganismNot specified

UniProt P07437

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–444 Chain D; UniProt 1–444 Chain F; UniProt 1–444 Chain Q; UniProt 1–444 Not recorded Tubulin alpha-1B chain × 4 (P68363) G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 4 MG MAGNESIUM ION × 8 GTP GUANOSINE-5'-TRIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE;Double-cycled GMPCPP microtubules were diluted to 2.5uM in Brb80 buffer. 5 ul of microtubules were applied to glow-discharged cryo-EM grid and allowed to absorb for 30 sec. 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBB5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–444; UniProt 1–444 Author chain D; PDBConstruct 1–444; UniProt 1–444 Author chain F; PDBConstruct 1–444; UniProt 1–444 Author chain Q; PDBConstruct 1–444; UniProt 1–444

Tubulin alpha-1B chain

OrganismNot specified

UniProt P68363

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–451 Chain C; UniProt 1–451 Chain E; UniProt 1–451 Chain I; UniProt 1–451 Not recorded Tubulin beta chain × 4 (P07437) G2P PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 4 MG MAGNESIUM ION × 8 GTP GUANOSINE-5'-TRIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE;Double-cycled GMPCPP microtubules were diluted to 2.5uM in Brb80 buffer. 5 ul of microtubules were applied to glow-discharged cryo-EM grid and allowed to absorb for 30 sec. 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.

38 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBA1B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–451; UniProt 1–451 Author chain C; PDBConstruct 1–451; UniProt 1–451 Author chain E; PDBConstruct 1–451; UniProt 1–451 Author chain I; 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 9cmm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9cmm
Deposition date deposition_date2024-07-15
Structure title titleTwo protofilament structure of alpha1B and betaI/IVb microtubule bound to GMPCPP
Keywords keywordshuman microtubule, tubulin isoforms, cytoskeleton, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier57.97
Radius of gyration Rg (electron density) rg_electron58.21
Forward intensity I(0) i02260690000.00
Molecular weight molecular_weight388310.0 kDa
Excluded volume excluded_volume480590 ų
Envelope volume envelope_volume646570 ų
Hydration-shell volume shell_volume93477 ų
Envelope diameter envelope_diameter209.4
Shell Rg shell_rg58.69
Envelope Rg envelope_rg57.54
Shape Rg shape_rg58.22
Total Rg total_rg58.19
Total atoms total_atoms27249
Residues n_residues3464
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 dmax204.3
Rg (real space) rg_real58.27
Rg uncertainty (real space) rg_real_error2.33
I(0) (real space) i0_real2.2610e+09
I(0) uncertainty (real space) i0_real_error4.5000e+07
Rg (reciprocal space) rg_reciprocal57.70
I(0) (reciprocal space) i0_reciprocal2259000000.0000
Solution quality estimate total_estimate0.8466
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.1
Skewness Skewness skewness0.446
Kurtosis Kurtosis kurtosis-0.346
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha127300000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.791; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.910; Smooth: 0.719

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)