8bmt

Structure of GroEL:GroES-ATP complex plunge frozen 200 ms after reaction initiation

Method: ELECTRON MICROSCOPY Dmax: 212.2 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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain A; UniProt 1–548 Chain BA; UniProt 1–548 Chain C; UniProt 1–548 Chain E; UniProt 1–548 Chain G; UniProt 1–548 Chain I; UniProt 1–548 Chain J; UniProt 1–548 Chain L; UniProt 1–548 Chain N; UniProt 1–548 Chain P; UniProt 1–548 Chain R; UniProt 1–548 Chain T; UniProt 1–548 Chain X; UniProt 1–548 Chain Z; UniProt 1–548 Not recorded Co-chaperonin GroES × 14 (P0A6F9) MG MAGNESIUM ION × 14 K POTASSIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE 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 BA; PDBConstruct 1–548; UniProt 1–548 Author chain C; PDBConstruct 1–548; UniProt 1–548 Author chain E; PDBConstruct 1–548; UniProt 1–548 Author chain G; PDBConstruct 1–548; UniProt 1–548 Author chain I; PDBConstruct 1–548; UniProt 1–548 Author chain J; PDBConstruct 1–548; UniProt 1–548 Author chain L; PDBConstruct 1–548; UniProt 1–548 Author chain N; PDBConstruct 1–548; UniProt 1–548 Author chain P; PDBConstruct 1–548; UniProt 1–548 Author chain R; PDBConstruct 1–548; UniProt 1–548 Author chain T; PDBConstruct 1–548; UniProt 1–548 Author chain X; PDBConstruct 1–548; UniProt 1–548 Author chain Z; 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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain AA; UniProt 2–97 Chain B; UniProt 2–97 Chain CA; UniProt 2–97 Chain D; UniProt 2–97 Chain F; UniProt 2–97 Chain H; UniProt 2–97 Chain K; UniProt 2–97 Chain M; UniProt 2–97 Chain O; UniProt 2–97 Chain Q; UniProt 2–97 Chain S; UniProt 2–97 Chain V; UniProt 2–97 Chain W; UniProt 2–97 Chain Y; UniProt 2–97 Not recorded Chaperonin GroEL × 14 (P0A6F5) MG MAGNESIUM ION × 14 K POTASSIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE 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 AA; PDBConstruct 3–98; UniProt 2–97 Author chain B; PDBConstruct 3–98; UniProt 2–97 Author chain CA; PDBConstruct 3–98; UniProt 2–97 Author chain D; PDBConstruct 3–98; UniProt 2–97 Author chain F; PDBConstruct 3–98; UniProt 2–97 Author chain H; PDBConstruct 3–98; UniProt 2–97 Author chain K; PDBConstruct 3–98; UniProt 2–97 Author chain M; PDBConstruct 3–98; UniProt 2–97 Author chain O; PDBConstruct 3–98; UniProt 2–97 Author chain Q; PDBConstruct 3–98; UniProt 2–97 Author chain S; PDBConstruct 3–98; UniProt 2–97 Author chain V; PDBConstruct 3–98; UniProt 2–97 Author chain W; PDBConstruct 3–98; UniProt 2–97 Author chain Y; PDBConstruct 3–98; UniProt 2–97

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 8bmt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8bmt
Deposition date deposition_date2022-11-10
Structure title titleStructure of GroEL:GroES-ATP complex plunge frozen 200 ms after reaction initiation
Keywords keywordsGroEL, GroES, CHAPERONE; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier72.03
Radius of gyration Rg (electron density) rg_electron72.33
Forward intensity I(0) i012070600000.00
Molecular weight molecular_weight921190.0 kDa
Excluded volume excluded_volume1151600 ų
Envelope volume envelope_volume2033600 ų
Hydration-shell volume shell_volume229440 ų
Envelope diameter envelope_diameter246.5
Shell Rg shell_rg79.29
Envelope Rg envelope_rg69.24
Shape Rg shape_rg72.39
Total Rg total_rg72.21
Total atoms total_atoms64372
Residues n_residues8680
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 dmax212.2
Rg (real space) rg_real71.23
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real1.1980e+10
I(0) uncertainty (real space) i0_real_error2.2740e+08
Rg (reciprocal space) rg_reciprocal72.32
I(0) (reciprocal space) i0_reciprocal12080000000.0000
Solution quality estimate total_estimate0.8289
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary96.5
Skewness Skewness skewness0.334
Kurtosis Kurtosis kurtosis0.018
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0554
Highest regularization parameter α highest_alpha2539000000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.799; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.400

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)