8p4m

CryoEM structure of a C7-symmetrical GroEL7-GroES7 cage in presence of ADP-BeFx

Method: ELECTRON MICROSCOPY Dmax: 141.4 Å Quality: GOOD

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

Chaperonin GroEL

Escherichia coli

UniProt P0A6F5

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain A; UniProt 1–548 Chain B; UniProt 1–548 Chain C; UniProt 1–548 Chain D; UniProt 1–548 Chain E; UniProt 1–548 Chain F; UniProt 1–548 Chain G; UniProt 1–548 Not recorded Co-chaperonin GroES × 7 (P0A6F9) ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7 BEF BERYLLIUM TRIFLUORIDE ION × 7 K POTASSIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;5.9 mM n-octyl-beta-D-glucopyranoside were added before vitrification Resolution 2.50 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.

81 other PDB entries and 95 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CH60_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–548; UniProt 1–548 Author chain B; PDBConstruct 1–548; UniProt 1–548 Author chain C; PDBConstruct 1–548; UniProt 1–548 Author chain D; PDBConstruct 1–548; UniProt 1–548 Author chain E; PDBConstruct 1–548; UniProt 1–548 Author chain F; PDBConstruct 1–548; UniProt 1–548 Author chain G; PDBConstruct 1–548; UniProt 1–548

Co-chaperonin GroES

Escherichia coli

UniProt P0A6F9

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain O; UniProt 1–97 Chain P; UniProt 1–97 Chain Q; UniProt 1–97 Chain R; UniProt 1–97 Chain S; UniProt 1–97 Chain T; UniProt 1–97 Chain U; UniProt 1–97 Not recorded Chaperonin GroEL × 7 (P0A6F5) ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7 BEF BERYLLIUM TRIFLUORIDE ION × 7 K POTASSIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;5.9 mM n-octyl-beta-D-glucopyranoside were added before vitrification Resolution 2.50 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 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CH10_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain O; PDBConstruct 1–97; UniProt 1–97 Author chain P; PDBConstruct 1–97; UniProt 1–97 Author chain Q; PDBConstruct 1–97; UniProt 1–97 Author chain R; PDBConstruct 1–97; UniProt 1–97 Author chain S; PDBConstruct 1–97; UniProt 1–97 Author chain T; PDBConstruct 1–97; UniProt 1–97 Author chain U; PDBConstruct 1–97; UniProt 1–97

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 8p4m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8p4m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8p4m
Deposition date deposition_date2023-05-23
Structure title titleCryoEM structure of a C7-symmetrical GroEL7-GroES7 cage in presence of ADP-BeFx
Keywords keywordsChaperonin, Folding cage, proteostasis, heat shock, ATPase, CHAPERONE; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier58.19
Radius of gyration Rg (electron density) rg_electron57.32
Forward intensity I(0) i03025470000.00
Molecular weight molecular_weight457820.0 kDa
Excluded volume excluded_volume573270 ų
Envelope volume envelope_volume1011100 ų
Hydration-shell volume shell_volume146280 ų
Envelope diameter envelope_diameter151.3
Shell Rg shell_rg65.67
Envelope Rg envelope_rg51.85
Shape Rg shape_rg57.33
Total Rg total_rg57.52
Total atoms total_atoms31997
Residues n_residues4333
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 dmax141.4
Rg (real space) rg_real57.58
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real3.0250e+09
I(0) uncertainty (real space) i0_real_error5.3860e+07
Rg (reciprocal space) rg_reciprocal58.69
I(0) (reciprocal space) i0_reciprocal3031000000.0000
Solution quality estimate total_estimate0.8413
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary89.0
Skewness Skewness skewness-0.298
Kurtosis Kurtosis kurtosis-0.662
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha187300000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.981; Stabil: 0.999; 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 (7)

8. Citations (1)

9. Files and Curves (10)