7qj5

Structure of recombinant human gamma-Tubulin Ring Complex (spokes 1-14)

Method: ELECTRON MICROSCOPY Dmax: 338.8 Å Quality: EXCELLENT

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

Tubulin gamma-1 chain

Homo sapiens

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 heterocomplex Heteromer Protein × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain 1; UniProt 1–451 Chain 2; UniProt 1–451 Chain O; UniProt 1–451 Chain P; UniProt 1–451 Chain Q; UniProt 1–451 Chain R; UniProt 1–451 Chain S; UniProt 1–451 Chain T; UniProt 1–451 Chain U; UniProt 1–451 Chain V; UniProt 1–451 Chain W; UniProt 1–451 Chain X; UniProt 1–451 Chain Y; UniProt 1–451 Chain Z; UniProt 1–451 Not recorded actin, cytoplasmic 1 × 1 (A0A6I9HGD1) Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Gamma-tubulin complex component 3 × 9 (Q96CW5) Mitotic-spindle organizing protein 1 × 6 (Q08AG7) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Gamma-tubulin complex component 5 × 2 (Q96RT8) Gamma-tubulin complex component 6 × 2 (Q96RT7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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 1; PDBConstruct 1–451; UniProt 1–451 Author chain 2; PDBConstruct 1–451; UniProt 1–451 Author chain O; PDBConstruct 1–451; UniProt 1–451 Author chain P; PDBConstruct 1–451; UniProt 1–451 Author chain Q; PDBConstruct 1–451; UniProt 1–451 Author chain R; PDBConstruct 1–451; UniProt 1–451 Author chain S; PDBConstruct 1–451; UniProt 1–451 Author chain T; PDBConstruct 1–451; UniProt 1–451 Author chain U; PDBConstruct 1–451; UniProt 1–451 Author chain V; PDBConstruct 1–451; UniProt 1–451 Author chain W; PDBConstruct 1–451; UniProt 1–451 Author chain X; PDBConstruct 1–451; UniProt 1–451 Author chain Y; PDBConstruct 1–451; UniProt 1–451 Author chain Z; PDBConstruct 1–451; UniProt 1–451

actin, cytoplasmic 1

Homo sapiens

UniProt A0A6I9HGD1

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 × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain e; UniProt 1–375 Not recorded Tubulin gamma-1 chain × 14 (P23258) Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Gamma-tubulin complex component 3 × 9 (Q96CW5) Mitotic-spindle organizing protein 1 × 6 (Q08AG7) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Gamma-tubulin complex component 5 × 2 (Q96RT8) Gamma-tubulin complex component 6 × 2 (Q96RT7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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.

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

View Construct and Data Evidence
UniProt name A0A6I9HGD1_GEOFO
Isoform
PDB entities 2
Chains and sequence ranges Author chain e; PDBConstruct 1–375; UniProt 1–375

Gamma-tubulin complex component 2

Homo sapiens

UniProt Q9BSJ2

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 × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain A; UniProt 1–902 Chain C; UniProt 1–902 Chain E; UniProt 1–902 Chain G; UniProt 1–902 Chain M; UniProt 1–902 Not recorded Tubulin gamma-1 chain × 14 (P23258) actin, cytoplasmic 1 × 1 (A0A6I9HGD1) Gamma-tubulin complex component 3 × 9 (Q96CW5) Mitotic-spindle organizing protein 1 × 6 (Q08AG7) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Gamma-tubulin complex component 5 × 2 (Q96RT8) Gamma-tubulin complex component 6 × 2 (Q96RT7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCP2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–902; UniProt 1–902 Author chain C; PDBConstruct 1–902; UniProt 1–902 Author chain E; PDBConstruct 1–902; UniProt 1–902 Author chain G; PDBConstruct 1–902; UniProt 1–902 Author chain M; PDBConstruct 1–902; UniProt 1–902

Gamma-tubulin complex component 3

Homo sapiens

UniProt Q96CW5

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 × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain B; UniProt 1–907 Chain D; UniProt 1–907 Chain F; UniProt 1–907 Chain H; UniProt 1–907 Chain N; UniProt 1–907 Chain a; UniProt 1–907 Chain f; UniProt 1–907 Chain h; UniProt 1–907 Chain j; UniProt 1–907 Not recorded Tubulin gamma-1 chain × 14 (P23258) actin, cytoplasmic 1 × 1 (A0A6I9HGD1) Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Mitotic-spindle organizing protein 1 × 6 (Q08AG7) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Gamma-tubulin complex component 5 × 2 (Q96RT8) Gamma-tubulin complex component 6 × 2 (Q96RT7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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.

27 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCP3_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–907; UniProt 1–907 Author chain D; PDBConstruct 1–907; UniProt 1–907 Author chain F; PDBConstruct 1–907; UniProt 1–907 Author chain H; PDBConstruct 1–907; UniProt 1–907 Author chain N; PDBConstruct 1–907; UniProt 1–907 Author chain a; PDBConstruct 1–907; UniProt 1–907 Author chain f; PDBConstruct 1–907; UniProt 1–907 Author chain h; PDBConstruct 1–907; UniProt 1–907 Author chain j; PDBConstruct 1–907; UniProt 1–907

Mitotic-spindle organizing protein 1

Homo sapiens

UniProt Q08AG7

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 × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain b; UniProt 1–82 Chain d; UniProt 1–82 Chain g; UniProt 1–82 Chain i; UniProt 1–82 Chain k; UniProt 1–82 Chain m; UniProt 1–82 Not recorded Tubulin gamma-1 chain × 14 (P23258) actin, cytoplasmic 1 × 1 (A0A6I9HGD1) Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Gamma-tubulin complex component 3 × 9 (Q96CW5) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Gamma-tubulin complex component 5 × 2 (Q96RT8) Gamma-tubulin complex component 6 × 2 (Q96RT7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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.

26 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MZT1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain b; PDBConstruct 1–82; UniProt 1–82 Author chain d; PDBConstruct 1–82; UniProt 1–82 Author chain g; PDBConstruct 1–82; UniProt 1–82 Author chain i; PDBConstruct 1–82; UniProt 1–82 Author chain k; PDBConstruct 1–82; UniProt 1–82 Author chain m; PDBConstruct 1–82; UniProt 1–82

Gamma-tubulin complex component 4

Homo sapiens

UniProt Q9UGJ1

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 × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain I; UniProt 1–667 Chain K; UniProt 1–667 Not recorded Tubulin gamma-1 chain × 14 (P23258) actin, cytoplasmic 1 × 1 (A0A6I9HGD1) Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Gamma-tubulin complex component 3 × 9 (Q96CW5) Mitotic-spindle organizing protein 1 × 6 (Q08AG7) Gamma-tubulin complex component 5 × 2 (Q96RT8) Gamma-tubulin complex component 6 × 2 (Q96RT7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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.

28 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCP4_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain I; PDBConstruct 1–667; UniProt 1–667 Author chain K; PDBConstruct 1–667; UniProt 1–667

Gamma-tubulin complex component 5

Homo sapiens

UniProt Q96RT8

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 × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain J; UniProt 1–1024 Chain l; UniProt 1–1024 Not recorded Tubulin gamma-1 chain × 14 (P23258) actin, cytoplasmic 1 × 1 (A0A6I9HGD1) Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Gamma-tubulin complex component 3 × 9 (Q96CW5) Mitotic-spindle organizing protein 1 × 6 (Q08AG7) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Gamma-tubulin complex component 6 × 2 (Q96RT7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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.

28 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCP5_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain J; PDBConstruct 1–1024; UniProt 1–1024 Author chain l; PDBConstruct 1–1024; UniProt 1–1024

Gamma-tubulin complex component 6

Homo sapiens

UniProt Q96RT7

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 × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain L; UniProt 1–1819 Chain c; UniProt 1–1819 Not recorded Tubulin gamma-1 chain × 14 (P23258) actin, cytoplasmic 1 × 1 (A0A6I9HGD1) Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Gamma-tubulin complex component 3 × 9 (Q96CW5) Mitotic-spindle organizing protein 1 × 6 (Q08AG7) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Gamma-tubulin complex component 5 × 2 (Q96RT8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.70 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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCP6_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain L; PDBConstruct 1–1819; UniProt 1–1819 Author chain c; PDBConstruct 1–1819; UniProt 1–1819

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 7qj5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7qj5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7qj5
Deposition date deposition_date2021-12-16
Structure title titleStructure of recombinant human gamma-Tubulin Ring Complex (spokes 1-14)
Keywords keywordsAssembly, Intermediate, Complex, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron115.60
Forward intensity I(0) i042547100000.00
Molecular weight molecular_weight1797700.0 kDa
Excluded volume excluded_volume2262400 ų
Envelope volume envelope_volume4664900 ų
Hydration-shell volume shell_volume339110 ų
Envelope diameter envelope_diameter346.8
Shell Rg shell_rg116.80
Envelope Rg envelope_rg105.30
Shape Rg shape_rg115.60
Total Rg total_rg115.70
Total atoms total_atoms126600
Residues n_residues15641
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 dmax338.8
Rg (real space) rg_real116.70
Rg uncertainty (real space) rg_real_error1.33
I(0) (real space) i0_real4.1540e+10
I(0) uncertainty (real space) i0_real_error8.3850e+08
Rg (reciprocal space) rg_reciprocal118.40
I(0) (reciprocal space) i0_reciprocal42730000000.0000
Solution quality estimate total_estimate0.9029
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary156.4
Skewness Skewness skewness-0.015
Kurtosis Kurtosis kurtosis-0.803
Angular range angular_range— – 0.0650 −1
Current regularization parameter α current_alpha1.7440
Highest regularization parameter α highest_alpha1075000000.0000
Real-space data points n_real_points14
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.997; Stabil: 0.922; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)