6v5v

Structure of gamma-tubulin in the native human gamma-tubulin ring complex

Method: ELECTRON MICROSCOPY Dmax: 69.3 Å Quality: EXCELLENT

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

Tubulin gamma-1 chain

OrganismNot specified

UniProt P23258

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain g; UniProt 1–451 Not recorded GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

31 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBG1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain g; 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 6v5v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6v5v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6v5v
Deposition date deposition_date2019-12-04
Structure title titleStructure of gamma-tubulin in the native human gamma-tubulin ring complex
Keywords keywords;Tubulin, gamma-tubulin, gamma-tubulin ring complex, gTuRC, g-TuRC, microtubule, microtubule nucleation, single particle cryo-EM structure, STRUCTURAL PROTEIN ;; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier22.36
Radius of gyration Rg (electron density) rg_electron21.04
Forward intensity I(0) i030930600.00
Molecular weight molecular_weight42363.0 kDa
Excluded volume excluded_volume52993 ų
Envelope volume envelope_volume65582 ų
Hydration-shell volume shell_volume25435 ų
Envelope diameter envelope_diameter70.1
Shell Rg shell_rg28.54
Envelope Rg envelope_rg21.31
Shape Rg shape_rg21.06
Total Rg total_rg21.95
Total atoms total_atoms2979
Residues n_residues369
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 dmax69.3
Rg (real space) rg_real22.23
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real3.0930e+07
I(0) uncertainty (real space) i0_real_error4.1030e+05
Rg (reciprocal space) rg_reciprocal22.26
I(0) (reciprocal space) i0_reciprocal30930000.0000
Solution quality estimate total_estimate0.9001
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.4
Skewness Skewness skewness0.165
Kurtosis Kurtosis kurtosis-0.392
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6157000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id6v5vg01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1440 — Tubulin/FtsZ, GTPase domain
Domain ID domain_id6v5vg02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily20 — Tubulin/FtsZ, C-terminal domain
Domain ID domain_id6v5vg03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily600 — Helix hairpin bin

8. Citations (1)

9. Files and Curves (10)