6x0v

Structure of MZT2/GCP-NHD and CDK5Rap2 at position 13 of the gamma-TuRC

Method: ELECTRON MICROSCOPY Dmax: 70.0 Å Quality: EXCELLENT

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

Mitotic-spindle organizing protein 2A

OrganismNot specified

UniProt Q6P582

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–158 Not recorded Gamma-tubulin complex component 2 × 1 (Q9BSJ2) Centrosome protein Cep215 × 2 (Q66GT8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MZT2A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–158; UniProt 1–158

Gamma-tubulin complex component 2

OrganismNot specified

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 1–930 Not recorded Mitotic-spindle organizing protein 2A × 1 (Q6P582) Centrosome protein Cep215 × 2 (Q66GT8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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 2
Chains and sequence ranges Author chain F; PDBConstruct 1–930; UniProt 1–930

Centrosome protein Cep215

OrganismNot specified

UniProt Q66GT8

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 1–1893 Chain H; UniProt 1–1893 Not recorded Mitotic-spindle organizing protein 2A × 1 (Q6P582) Gamma-tubulin complex component 2 × 1 (Q9BSJ2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q66GT8_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–1893; UniProt 1–1893 Author chain H; PDBConstruct 1–1893; UniProt 1–1893

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 6x0v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6x0v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6x0v
Deposition date deposition_date2020-05-17
Structure title titleStructure of MZT2/GCP-NHD and CDK5Rap2 at position 13 of the gamma-TuRC
Keywords keywordsgamma-TuRC, MZT2, GCP, CDK5Rap2, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier21.90
Radius of gyration Rg (electron density) rg_electron21.44
Forward intensity I(0) i08000860.00
Molecular weight molecular_weight18645.0 kDa
Excluded volume excluded_volume22417 ų
Envelope volume envelope_volume35451 ų
Hydration-shell volume shell_volume15382 ų
Envelope diameter envelope_diameter71.8
Shell Rg shell_rg25.50
Envelope Rg envelope_rg20.86
Shape Rg shape_rg21.39
Total Rg total_rg22.21
Total atoms total_atoms1384
Residues n_residues211
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 dmax70.0
Rg (real space) rg_real21.91
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real8.0010e+06
I(0) uncertainty (real space) i0_real_error1.1080e+05
Rg (reciprocal space) rg_reciprocal21.91
I(0) (reciprocal space) i0_reciprocal8001000.0000
Solution quality estimate total_estimate0.9057
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.9
Skewness Skewness skewness0.251
Kurtosis Kurtosis kurtosis-0.604
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1198000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)