3zpz

Visualizing GroEL-ES in the Act of Encapsulating a Non-Native Substrate Protein

Method: ELECTRON MICROSCOPY Dmax: 195.3 Å Quality: GOOD

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

60 KDA CHAPERONIN

ESCHERICHIA COLI BL21

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 × 21 PDB declaration: 21-meric(21) Consistent with protein copy count Chain A; UniProt 2–527 Chain B; UniProt 2–527 Chain C; UniProt 2–527 Chain D; UniProt 2–527 Chain E; UniProt 2–527 Chain F; UniProt 2–527 Chain G; UniProt 2–527 Chain H; UniProt 2–527 Chain I; UniProt 2–527 Chain J; UniProt 2–527 Chain K; UniProt 2–527 Chain L; UniProt 2–527 Chain M; UniProt 2–527 Chain N; UniProt 2–527 Not recorded 10 KDA CHAPERONIN × 7 (P0A6F9) MG MAGNESIUM ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 7 ELECTRON MICROSCOPY cryo-EM buffer:50 MM HEPES, 5 MM KOAC, 10 MM MG(OAC)2, 2 MM DTT;pH 7.6;50 MM HEPES, 5 MM KOAC, 10 MM MG(OAC)2, 2 MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 95, TEMPERATURE- 98, INSTRUMENT- FEI VITROBOT MARK III, METHOD- BLOT FOR 1 SECOND BEFORE PLUNGING, Resolution 8.90 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 1–526; UniProt 2–527 Author chain B; PDBConstruct 1–526; UniProt 2–527 Author chain C; PDBConstruct 1–526; UniProt 2–527 Author chain D; PDBConstruct 1–526; UniProt 2–527 Author chain E; PDBConstruct 1–526; UniProt 2–527 Author chain F; PDBConstruct 1–526; UniProt 2–527 Author chain G; PDBConstruct 1–526; UniProt 2–527 Author chain H; PDBConstruct 1–526; UniProt 2–527 Author chain I; PDBConstruct 1–526; UniProt 2–527 Author chain J; PDBConstruct 1–526; UniProt 2–527 Author chain K; PDBConstruct 1–526; UniProt 2–527 Author chain L; PDBConstruct 1–526; UniProt 2–527 Author chain M; PDBConstruct 1–526; UniProt 2–527 Author chain N; PDBConstruct 1–526; UniProt 2–527

10 KDA CHAPERONIN

ESCHERICHIA COLI K-12

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 × 21 PDB declaration: 21-meric(21) 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 60 KDA CHAPERONIN × 14 (P0A6F5) MG MAGNESIUM ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 7 ELECTRON MICROSCOPY cryo-EM buffer:50 MM HEPES, 5 MM KOAC, 10 MM MG(OAC)2, 2 MM DTT;pH 7.6;50 MM HEPES, 5 MM KOAC, 10 MM MG(OAC)2, 2 MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 95, TEMPERATURE- 98, INSTRUMENT- FEI VITROBOT MARK III, METHOD- BLOT FOR 1 SECOND BEFORE PLUNGING, Resolution 8.90 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 3zpz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3zpz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3zpz
Deposition date deposition_date2013-03-04
Structure title titleVisualizing GroEL-ES in the Act of Encapsulating a Non-Native Substrate Protein
Keywords keywordsCHAPERONE, PROTEIN FOLDING, HETEROGENEITY; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier68.91
Radius of gyration Rg (electron density) rg_electron68.67
Forward intensity I(0) i010180500000.00
Molecular weight molecular_weight847780.0 kDa
Excluded volume excluded_volume1061200 ų
Envelope volume envelope_volume1866600 ų
Hydration-shell volume shell_volume219150 ų
Envelope diameter envelope_diameter209.9
Shell Rg shell_rg78.05
Envelope Rg envelope_rg64.80
Shape Rg shape_rg68.70
Total Rg total_rg68.71
Total atoms total_atoms59276
Residues n_residues8029
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 dmax195.3
Rg (real space) rg_real68.64
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real1.0180e+10
I(0) uncertainty (real space) i0_real_error1.9360e+08
Rg (reciprocal space) rg_reciprocal69.76
I(0) (reciprocal space) i0_reciprocal10200000000.0000
Solution quality estimate total_estimate0.8278
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary93.4
Skewness Skewness skewness0.125
Kurtosis Kurtosis kurtosis-0.296
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha3173000000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.056

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)