8sgq

CCT G beta 5 complex intermediate state

Method: ELECTRON MICROSCOPY Dmax: 218.4 Å Quality: GOOD

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

T-complex protein 1 subunit zeta

OrganismNot specified

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: hexadecameric(16) Consistent with protein copy count Chain Z; UniProt 17–524 Chain z; UniProt 17–524 Not recorded T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit eta, N-terminally processed × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) ADP ADENOSINE-5'-DIPHOSPHATE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 1
Chains and sequence ranges Author chain Z; PDBConstruct 1–508; UniProt 17–524 Author chain z; PDBConstruct 1–508; UniProt 17–524

T-complex protein 1 subunit alpha

OrganismNot specified

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: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 2–537 Chain a; UniProt 2–537 Not recorded T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit eta, N-terminally processed × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) ADP ADENOSINE-5'-DIPHOSPHATE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 2
Chains and sequence ranges Author chain A; PDBConstruct 1–536; UniProt 2–537 Author chain a; PDBConstruct 1–536; UniProt 2–537

T-complex protein 1 subunit gamma

OrganismNot specified

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: hexadecameric(16) Consistent with protein copy count Chain G; UniProt 3–530 Chain g; UniProt 3–530 Not recorded T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit eta, N-terminally processed × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) ADP ADENOSINE-5'-DIPHOSPHATE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 3
Chains and sequence ranges Author chain G; PDBConstruct 1–528; UniProt 3–530 Author chain g; PDBConstruct 1–528; UniProt 3–530

T-complex protein 1 subunit eta, N-terminally processed

OrganismNot specified

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: hexadecameric(16) Consistent with protein copy count Chain H; UniProt 12–525 Chain h; UniProt 12–525 Not recorded T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) ADP ADENOSINE-5'-DIPHOSPHATE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 4
Chains and sequence ranges Author chain H; PDBConstruct 1–514; UniProt 12–525 Author chain h; PDBConstruct 1–514; UniProt 12–525

T-complex protein 1 subunit theta

OrganismNot specified

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: hexadecameric(16) Consistent with protein copy count Chain Q; UniProt 29–526 Chain q; UniProt 29–526 Not recorded T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit eta, N-terminally processed × 2 (Q99832) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) ADP ADENOSINE-5'-DIPHOSPHATE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 5
Chains and sequence ranges Author chain Q; PDBConstruct 1–498; UniProt 29–526 Author chain q; PDBConstruct 1–498; UniProt 29–526

T-complex protein 1 subunit beta

OrganismNot specified

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: hexadecameric(16) Consistent with protein copy count Chain B; UniProt 2–527 Chain b; UniProt 2–527 Not recorded T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit eta, N-terminally processed × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit delta × 2 (P50991) T-complex protein 1 subunit epsilon × 2 (P48643) ADP ADENOSINE-5'-DIPHOSPHATE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 6
Chains and sequence ranges Author chain B; PDBConstruct 1–526; UniProt 2–527 Author chain b; PDBConstruct 1–526; UniProt 2–527

T-complex protein 1 subunit delta

OrganismNot specified

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: hexadecameric(16) Consistent with protein copy count Chain D; UniProt 19–538 Chain d; UniProt 19–538 Not recorded T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit eta, N-terminally processed × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit epsilon × 2 (P48643) ADP ADENOSINE-5'-DIPHOSPHATE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 7
Chains and sequence ranges Author chain D; PDBConstruct 1–520; UniProt 19–538 Author chain d; PDBConstruct 1–520; UniProt 19–538

T-complex protein 1 subunit epsilon

OrganismNot specified

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: hexadecameric(16) Consistent with protein copy count Chain E; UniProt 2–541 Chain e; UniProt 2–541 Not recorded T-complex protein 1 subunit zeta × 2 (P40227) T-complex protein 1 subunit alpha × 2 (P17987) T-complex protein 1 subunit gamma × 2 (P49368) T-complex protein 1 subunit eta, N-terminally processed × 2 (Q99832) T-complex protein 1 subunit theta × 2 (P50990) T-complex protein 1 subunit beta × 2 (P78371) T-complex protein 1 subunit delta × 2 (P50991) ADP ADENOSINE-5'-DIPHOSPHATE × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 8
Chains and sequence ranges Author chain E; PDBConstruct 1–540; UniProt 2–541 Author chain e; PDBConstruct 1–540; UniProt 2–541

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 8sgq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8sgq
Deposition date deposition_date2023-04-12
Structure title titleCCT G beta 5 complex intermediate state
Keywords keywordsCCT, Gb5, complex, open, CHAPERONE; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier70.39
Radius of gyration Rg (electron density) rg_electron69.78
Forward intensity I(0) i011047900000.00
Molecular weight molecular_weight888930.0 kDa
Excluded volume excluded_volume1114100 ų
Envelope volume envelope_volume2015000 ų
Hydration-shell volume shell_volume230980 ų
Envelope diameter envelope_diameter214.1
Shell Rg shell_rg82.16
Envelope Rg envelope_rg64.48
Shape Rg shape_rg69.79
Total Rg total_rg69.92
Total atoms total_atoms62154
Residues n_residues8092
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 dmax218.4
Rg (real space) rg_real69.94
Rg uncertainty (real space) rg_real_error1.61
I(0) (real space) i0_real1.1050e+10
I(0) uncertainty (real space) i0_real_error2.2370e+08
Rg (reciprocal space) rg_reciprocal71.84
I(0) (reciprocal space) i0_reciprocal11090000000.0000
Solution quality estimate total_estimate0.8431
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary109.2
Skewness Skewness skewness-0.181
Kurtosis Kurtosis kurtosis-0.559
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2337000000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.738; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.924; Smooth: 0.817

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)