6wsg

ClpX-ClpP complex bound to ssrA-tagged GFP, intermediate complex

Method: ELECTRON MICROSCOPY Dmax: 146.2 Å Quality: GOOD

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

ATP-dependent Clp protease ATP-binding subunit ClpX

Escherichia coli

UniProt P0A6H1

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 62–424 Chain B; UniProt 62–424 Chain C; UniProt 62–424 Chain D; UniProt 62–424 Chain E; UniProt 62–424 Chain F; UniProt 62–424 Fragment:UNP residues 62-424 ATP-dependent Clp protease proteolytic subunit × 7 (P0A6G7) Green fluorescent protein, + ssrA tag × 1 (P42212) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.16 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.

20 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CLPX_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 26–388; UniProt 62–424 Author chain B; PDBConstruct 26–388; UniProt 62–424 Author chain C; PDBConstruct 26–388; UniProt 62–424 Author chain D; PDBConstruct 26–388; UniProt 62–424 Author chain E; PDBConstruct 26–388; UniProt 62–424 Author chain F; PDBConstruct 26–388; UniProt 62–424

ATP-dependent Clp protease proteolytic subunit

Escherichia coli

UniProt P0A6G7

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 H; UniProt 16–207 Chain I; UniProt 16–207 Chain J; UniProt 16–207 Chain K; UniProt 16–207 Chain L; UniProt 16–207 Chain M; UniProt 16–207 Chain N; UniProt 16–207 Fragment:UNP residues 16-207 ATP-dependent Clp protease ATP-binding subunit ClpX × 6 (P0A6H1) Green fluorescent protein, + ssrA tag × 1 (P42212) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.16 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.

18 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CLPP_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–192; UniProt 16–207 Author chain I; PDBConstruct 1–192; UniProt 16–207 Author chain J; PDBConstruct 1–192; UniProt 16–207 Author chain K; PDBConstruct 1–192; UniProt 16–207 Author chain L; PDBConstruct 1–192; UniProt 16–207 Author chain M; PDBConstruct 1–192; UniProt 16–207 Author chain N; PDBConstruct 1–192; UniProt 16–207

Green fluorescent protein, + ssrA tag

synthetic construct

UniProt P42212

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 S; UniProt 3–229 Not recorded ATP-dependent Clp protease ATP-binding subunit ClpX × 6 (P0A6H1) ATP-dependent Clp protease proteolytic subunit × 7 (P0A6G7) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.16 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 3
Chains and sequence ranges Author chain S; PDBConstruct 27–253; UniProt 3–229

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 6wsg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6wsg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6wsg
Deposition date deposition_date2020-04-30
Structure title titleClpX-ClpP complex bound to ssrA-tagged GFP, intermediate complex
Keywords keywordsProtein degradation, AAA+ protease complex, CHAPERONE; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.15
Radius of gyration Rg (electron density) rg_electron47.22
Forward intensity I(0) i01930790000.00
Molecular weight molecular_weight369510.0 kDa
Excluded volume excluded_volume464400 ų
Envelope volume envelope_volume641500 ų
Hydration-shell volume shell_volume107400 ų
Envelope diameter envelope_diameter150.4
Shell Rg shell_rg55.85
Envelope Rg envelope_rg46.17
Shape Rg shape_rg47.25
Total Rg total_rg47.43
Total atoms total_atoms52140
Residues n_residues3334
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 dmax146.2
Rg (real space) rg_real47.72
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real1.9310e+09
I(0) uncertainty (real space) i0_real_error2.9970e+07
Rg (reciprocal space) rg_reciprocal48.15
I(0) (reciprocal space) i0_reciprocal1932000000.0000
Solution quality estimate total_estimate0.8819
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.5
Skewness Skewness skewness0.030
Kurtosis Kurtosis kurtosis-0.498
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha457200000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.952; Smooth: 0.810

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)