8i6j

The focused refinement of CCT3-PhLP2A from TRiC-PhLP2A complex in the open state

Method: ELECTRON MICROSCOPY Dmax: 109.5 Å Quality: GOOD

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

Phosducin-like protein 3

Homo sapiens

UniProt Q9H2J4

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain Q; UniProt 1–239 Not recorded T-complex protein 1 subunit gamma × 1 (P49368) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.82 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PDCL3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain Q; PDBConstruct 1–239; UniProt 1–239

T-complex protein 1 subunit gamma

Homo sapiens

UniProt P49368

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–545 Not recorded Phosducin-like protein 3 × 1 (Q9H2J4) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.82 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.

65 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPG_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–545; UniProt 1–545

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 8i6j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8i6j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8i6j
Deposition date deposition_date2023-01-28
Structure title titleThe focused refinement of CCT3-PhLP2A from TRiC-PhLP2A complex in the open state
Keywords keywordschaperonin complex, CHAPERONE, cochaperone; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.16
Radius of gyration Rg (electron density) rg_electron32.54
Forward intensity I(0) i092305600.00
Molecular weight molecular_weight75606.0 kDa
Excluded volume excluded_volume94844 ų
Envelope volume envelope_volume140700 ų
Hydration-shell volume shell_volume36743 ų
Envelope diameter envelope_diameter110.6
Shell Rg shell_rg38.77
Envelope Rg envelope_rg31.73
Shape Rg shape_rg32.57
Total Rg total_rg33.04
Total atoms total_atoms5287
Residues n_residues670
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 dmax109.5
Rg (real space) rg_real33.16
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real9.2310e+07
I(0) uncertainty (real space) i0_real_error1.4900e+06
Rg (reciprocal space) rg_reciprocal33.17
I(0) (reciprocal space) i0_reciprocal92310000.0000
Solution quality estimate total_estimate0.8926
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.1
Skewness Skewness skewness0.288
Kurtosis Kurtosis kurtosis-0.453
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21260000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.893

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)