8vrd

Rigid body fitted model for free recombinant gamma tubulin ring complex.

Method: ELECTRON MICROSCOPY Dmax: 368.2 Å Quality: GOOD

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

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 × 34 PDB declaration: 34-meric(34) 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 O; UniProt 1–907 Not recorded TUBGCP6 protein × 3 (B2RWN4) Mitotic-spindle organizing protein 1 × 2 (Q08AG7) Actin, cytoplasmic 1 × 1 (P60709) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Tubulin gamma-1 chain × 14 (P23258) Isoform 2 of Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Gamma-tubulin complex component 5 × 1 (Q96RT8) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.00 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 1
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 O; PDBConstruct 1–907; UniProt 1–907

TUBGCP6 protein

Homo sapiens

UniProt B2RWN4

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain L; UniProt 1–1811 Chain P; UniProt 1–1811 Chain T; UniProt 1–1811 Not recorded Gamma-tubulin complex component 3 × 6 (Q96CW5) Mitotic-spindle organizing protein 1 × 2 (Q08AG7) Actin, cytoplasmic 1 × 1 (P60709) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Tubulin gamma-1 chain × 14 (P23258) Isoform 2 of Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Gamma-tubulin complex component 5 × 1 (Q96RT8) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.00 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2RWN4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 1–1811; UniProt 1–1811 Author chain P; PDBConstruct 1–1811; UniProt 1–1811 Author chain T; PDBConstruct 1–1811; UniProt 1–1811

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain Q; UniProt 1–82 Chain R; UniProt 1–82 Not recorded Gamma-tubulin complex component 3 × 6 (Q96CW5) TUBGCP6 protein × 3 (B2RWN4) Actin, cytoplasmic 1 × 1 (P60709) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Tubulin gamma-1 chain × 14 (P23258) Isoform 2 of Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Gamma-tubulin complex component 5 × 1 (Q96RT8) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.00 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 3
Chains and sequence ranges Author chain Q; PDBConstruct 1–82; UniProt 1–82 Author chain R; PDBConstruct 1–82; UniProt 1–82

Actin, cytoplasmic 1

Homo sapiens

UniProt P60709

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain S; UniProt 1–375 Not recorded Gamma-tubulin complex component 3 × 6 (Q96CW5) TUBGCP6 protein × 3 (B2RWN4) Mitotic-spindle organizing protein 1 × 2 (Q08AG7) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Tubulin gamma-1 chain × 14 (P23258) Isoform 2 of Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Gamma-tubulin complex component 5 × 1 (Q96RT8) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.00 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.

72 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTB_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain S; PDBConstruct 1–375; UniProt 1–375

Isoform 3 of 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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain A; UniProt 1–930 Chain C; UniProt 1–930 Chain E; UniProt 1–930 Chain G; UniProt 1–930 Chain M; UniProt 1–930 Not recorded Gamma-tubulin complex component 3 × 6 (Q96CW5) TUBGCP6 protein × 3 (B2RWN4) Mitotic-spindle organizing protein 1 × 2 (Q08AG7) Actin, cytoplasmic 1 × 1 (P60709) Tubulin gamma-1 chain × 14 (P23258) Isoform 2 of Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Gamma-tubulin complex component 5 × 1 (Q96RT8) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.00 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 Q9BSJ2-4
PDB entities 5
Chains and sequence ranges Author chain A; PDBConstruct 1–930; UniProt 1–930 Author chain C; PDBConstruct 1–930; UniProt 1–930 Author chain E; PDBConstruct 1–930; UniProt 1–930 Author chain G; PDBConstruct 1–930; UniProt 1–930 Author chain M; PDBConstruct 1–930; UniProt 1–930

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain a; UniProt 1–451 Chain b; UniProt 1–451 Chain c; UniProt 1–451 Chain d; UniProt 1–451 Chain e; UniProt 1–451 Chain f; UniProt 1–451 Chain g; UniProt 1–451 Chain h; UniProt 1–451 Chain i; UniProt 1–451 Chain j; UniProt 1–451 Chain k; UniProt 1–451 Chain l; UniProt 1–451 Chain m; UniProt 1–451 Chain n; UniProt 1–451 Not recorded Gamma-tubulin complex component 3 × 6 (Q96CW5) TUBGCP6 protein × 3 (B2RWN4) Mitotic-spindle organizing protein 1 × 2 (Q08AG7) Actin, cytoplasmic 1 × 1 (P60709) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Isoform 2 of Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Gamma-tubulin complex component 5 × 1 (Q96RT8) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.00 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 6
Chains and sequence ranges Author chain a; PDBConstruct 1–451; UniProt 1–451 Author chain b; PDBConstruct 1–451; UniProt 1–451 Author chain c; PDBConstruct 1–451; UniProt 1–451 Author chain d; PDBConstruct 1–451; UniProt 1–451 Author chain e; PDBConstruct 1–451; UniProt 1–451 Author chain f; PDBConstruct 1–451; UniProt 1–451 Author chain g; PDBConstruct 1–451; UniProt 1–451 Author chain h; PDBConstruct 1–451; UniProt 1–451 Author chain i; PDBConstruct 1–451; UniProt 1–451 Author chain j; PDBConstruct 1–451; UniProt 1–451 Author chain k; PDBConstruct 1–451; UniProt 1–451 Author chain l; PDBConstruct 1–451; UniProt 1–451 Author chain m; PDBConstruct 1–451; UniProt 1–451 Author chain n; PDBConstruct 1–451; UniProt 1–451

Isoform 2 of 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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain I; UniProt 1–666 Chain K; UniProt 1–666 Not recorded Gamma-tubulin complex component 3 × 6 (Q96CW5) TUBGCP6 protein × 3 (B2RWN4) Mitotic-spindle organizing protein 1 × 2 (Q08AG7) Actin, cytoplasmic 1 × 1 (P60709) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Tubulin gamma-1 chain × 14 (P23258) Gamma-tubulin complex component 5 × 1 (Q96RT8) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.00 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 Q9UGJ1-2
PDB entities 7
Chains and sequence ranges Author chain I; PDBConstruct 1–666; UniProt 1–666 Author chain K; PDBConstruct 1–666; UniProt 1–666

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain J; UniProt 1–1024 Not recorded Gamma-tubulin complex component 3 × 6 (Q96CW5) TUBGCP6 protein × 3 (B2RWN4) Mitotic-spindle organizing protein 1 × 2 (Q08AG7) Actin, cytoplasmic 1 × 1 (P60709) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Tubulin gamma-1 chain × 14 (P23258) Isoform 2 of Gamma-tubulin complex component 4 × 2 (Q9UGJ1) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.00 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 8
Chains and sequence ranges Author chain J; PDBConstruct 1–1024; UniProt 1–1024

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 8vrd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8vrd
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8vrd
Deposition date deposition_date2024-01-21
Structure title titleRigid body fitted model for free recombinant gamma tubulin ring complex.
Keywords keywordsComplex, 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_electron110.00
Forward intensity I(0) i018009100000.00
Molecular weight molecular_weight937940.0 kDa
Excluded volume excluded_volume1080500 ų
Envelope volume envelope_volume3648900 ų
Hydration-shell volume shell_volume284820 ų
Envelope diameter envelope_diameter333.3
Shell Rg shell_rg109.00
Envelope Rg envelope_rg98.39
Shape Rg shape_rg110.00
Total Rg total_rg110.00
Total atoms total_atoms67033
Residues n_residues13526
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 dmax368.2
Rg (real space) rg_real113.90
Rg uncertainty (real space) rg_real_error2.42
I(0) (real space) i0_real1.8010e+10
I(0) uncertainty (real space) i0_real_error4.3110e+08
Rg (reciprocal space) rg_reciprocal112.50
I(0) (reciprocal space) i0_reciprocal18110000000.0000
Solution quality estimate total_estimate0.8735
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary131.5
Skewness Skewness skewness0.171
Kurtosis Kurtosis kurtosis-0.371
Angular range angular_range— – 0.0700 −1
Current regularization parameter α current_alpha1.0260
Highest regularization parameter α highest_alpha689100000.0000
Real-space data points n_real_points15
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.908; Stabil: 0.903; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)