9e2s

Apo TRiC in closed conformation

Method: ELECTRON MICROSCOPY Dmax: 168.8 Å Quality: GOOD

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

T-complex protein 1 subunit theta

Homo sapiens

UniProt P50990

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 × 16 PDB declaration: 16-meric(16) Consistent with protein copy count Chain B; UniProt 1–547 Chain b; UniProt 1–547 Not recorded T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit zeta × 2 (P40227) MG MAGNESIUM ION × 16 ADP ADENOSINE-5'-DIPHOSPHATE × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

64 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPQ_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–547; UniProt 1–547 Author chain b; PDBConstruct 1–547; UniProt 1–547

T-complex protein 1 subunit eta

Homo sapiens

UniProt Q99832

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 × 16 PDB declaration: 16-meric(16) Consistent with protein copy count Chain C; UniProt 1–543 Chain c; UniProt 1–543 Not recorded T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit zeta × 2 (P40227) MG MAGNESIUM ION × 16 ADP ADENOSINE-5'-DIPHOSPHATE × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

63 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPH_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–553; UniProt 1–543 Author chain c; PDBConstruct 1–553; UniProt 1–543

T-complex protein 1 subunit epsilon

Homo sapiens

UniProt P48643

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 × 16 PDB declaration: 16-meric(16) Consistent with protein copy count Chain D; UniProt 1–541 Chain d; UniProt 1–541 Not recorded T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit zeta × 2 (P40227) MG MAGNESIUM ION × 16 ADP ADENOSINE-5'-DIPHOSPHATE × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

68 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPE_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–541; UniProt 1–541 Author chain d; PDBConstruct 1–541; UniProt 1–541

T-complex protein 1 subunit beta

Homo sapiens

UniProt P78371

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 × 16 PDB declaration: 16-meric(16) Consistent with protein copy count Chain E; UniProt 1–535 Chain e; UniProt 1–535 Not recorded T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit zeta × 2 (P40227) MG MAGNESIUM ION × 16 ADP ADENOSINE-5'-DIPHOSPHATE × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

64 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPB_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–535; UniProt 1–535 Author chain e; PDBConstruct 1–535; UniProt 1–535

T-complex protein 1 subunit delta

Homo sapiens

UniProt P50991

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 × 16 PDB declaration: 16-meric(16) Consistent with protein copy count Chain F; UniProt 1–539 Chain f; UniProt 1–539 Not recorded T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit zeta × 2 (P40227) MG MAGNESIUM ION × 16 ADP ADENOSINE-5'-DIPHOSPHATE × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

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

View Construct and Data Evidence
UniProt name TCPD_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 1–539; UniProt 1–539 Author chain f; PDBConstruct 1–539; UniProt 1–539

T-complex protein 1 subunit alpha

Homo sapiens

UniProt P17987

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 × 16 PDB declaration: 16-meric(16) Consistent with protein copy count Chain G; UniProt 1–556 Chain g; UniProt 1–556 Not recorded T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit zeta × 2 (P40227) MG MAGNESIUM ION × 16 ADP ADENOSINE-5'-DIPHOSPHATE × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

64 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPA_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain G; PDBConstruct 1–556; UniProt 1–556 Author chain g; PDBConstruct 1–556; UniProt 1–556

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 × 16 PDB declaration: 16-meric(16) Consistent with protein copy count Chain H; UniProt 1–545 Chain h; UniProt 1–545 Not recorded T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit zeta × 2 (P40227) MG MAGNESIUM ION × 16 ADP ADENOSINE-5'-DIPHOSPHATE × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

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 7
Chains and sequence ranges Author chain H; PDBConstruct 1–545; UniProt 1–545 Author chain h; PDBConstruct 1–545; UniProt 1–545

T-complex protein 1 subunit zeta

Homo sapiens

UniProt P40227

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 × 16 PDB declaration: 16-meric(16) Consistent with protein copy count Chain I; UniProt 1–531 Chain i; UniProt 1–531 Not recorded T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit eta × 2 (Q99832) T-complex protein 1 subunit epsilon × 2 (P48643) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit gamma × 2 (P49368) MG MAGNESIUM ION × 16 ADP ADENOSINE-5'-DIPHOSPHATE × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

64 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCPZ_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain I; PDBConstruct 1–531; UniProt 1–531 Author chain i; PDBConstruct 1–531; UniProt 1–531

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 9e2s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e2s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e2s
Deposition date deposition_date2024-10-22
最后修订 last_revision2025-10-08
Structure title titleApo TRiC in closed conformation
Keywords keywordshuman chaperonin, CHAPERONE; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier67.53
Radius of gyration Rg (electron density) rg_electron66.85
Forward intensity I(0) i011976700000.00
Molecular weight molecular_weight924800.0 kDa
Excluded volume excluded_volume1158700 ų
Envelope volume envelope_volume2031400 ų
Hydration-shell volume shell_volume240030 ų
Envelope diameter envelope_diameter187.7
Shell Rg shell_rg80.82
Envelope Rg envelope_rg61.81
Shape Rg shape_rg66.87
Total Rg total_rg66.98
Total atoms total_atoms64630
Residues n_residues8392
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 dmax168.8
Rg (real space) rg_real67.10
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real1.1980e+10
I(0) uncertainty (real space) i0_real_error1.8430e+08
Rg (reciprocal space) rg_reciprocal68.93
I(0) (reciprocal space) i0_reciprocal12020000000.0000
Solution quality estimate total_estimate0.8429
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary102.8
Skewness Skewness skewness-0.246
Kurtosis Kurtosis kurtosis-0.633
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8090000000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.987; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)