8f26

Structure of a 60mer DegP cage bound to the client protein hTRF1

Method: ELECTRON MICROSCOPY Dmax: 102.4 Å Quality: GOOD

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

Periplasmic serine endoprotease DegP

Escherichia coli (strain K12)

UniProt P0C0V0

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 × 180 PDB declaration: 180-meric(180) Consistent with protein copy count Chain A; UniProt 38–385 Chain D; UniProt 400–474 Fragment:protease and PDZ1 domains (UNP residues 38-385) Fragment:PDZ2 domain (UNP residues 400-474) Telomeric repeat-binding factor 1 × 60 (P54274) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 9.70 Å
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 38–385 Chain D; UniProt 400–474 Fragment:protease and PDZ1 domains (UNP residues 38-385) Fragment:PDZ2 domain (UNP residues 400-474) Telomeric repeat-binding factor 1 × 1 (P54274) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 9.70 Å
3 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 38–385 Chain D; UniProt 400–474 Fragment:protease and PDZ1 domains (UNP residues 38-385) Fragment:PDZ2 domain (UNP residues 400-474) Telomeric repeat-binding factor 1 × 5 (P54274) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 9.70 Å
4 Protein heterocomplex Heteromer Protein × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 38–385 Chain D; UniProt 400–474 Fragment:protease and PDZ1 domains (UNP residues 38-385) Fragment:PDZ2 domain (UNP residues 400-474) Telomeric repeat-binding factor 1 × 6 (P54274) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 9.70 Å
5 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 38–385 Chain D; UniProt 400–474 Fragment:protease and PDZ1 domains (UNP residues 38-385) Fragment:PDZ2 domain (UNP residues 400-474) Telomeric repeat-binding factor 1 × 1 (P54274) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 9.70 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.

18 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DEGP_ECOLI
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–348; UniProt 38–385 Author chain D; PDBConstruct 1–75; UniProt 400–474

Telomeric repeat-binding factor 1

Homo sapiens

UniProt P54274

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 × 180 PDB declaration: 180-meric(180) Consistent with protein copy count Chain a; UniProt 404–430 Fragment:UNP residues 404-430 Periplasmic serine endoprotease DegP × 60 (P0C0V0) Periplasmic serine endoprotease DegP × 60 (P0C0V0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 9.70 Å
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain a; UniProt 404–430 Fragment:UNP residues 404-430 Periplasmic serine endoprotease DegP × 1 (P0C0V0) Periplasmic serine endoprotease DegP × 1 (P0C0V0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 9.70 Å
3 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain a; UniProt 404–430 Fragment:UNP residues 404-430 Periplasmic serine endoprotease DegP × 5 (P0C0V0) Periplasmic serine endoprotease DegP × 5 (P0C0V0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 9.70 Å
4 Protein heterocomplex Heteromer Protein × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain a; UniProt 404–430 Fragment:UNP residues 404-430 Periplasmic serine endoprotease DegP × 6 (P0C0V0) Periplasmic serine endoprotease DegP × 6 (P0C0V0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 9.70 Å
5 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain a; UniProt 404–430 Fragment:UNP residues 404-430 Periplasmic serine endoprotease DegP × 1 (P0C0V0) Periplasmic serine endoprotease DegP × 1 (P0C0V0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 9.70 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.

57 other PDB entries and 69 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TERF1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain a; PDBConstruct 1–27; UniProt 404–430

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 8f26

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8f26
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8f26
Deposition date deposition_date2022-11-07
Structure title titleStructure of a 60mer DegP cage bound to the client protein hTRF1
Keywords keywordsProtease, chaperone, hydrolase, cage, complex; CHAPERONE, HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier26.35
Radius of gyration Rg (electron density) rg_electron26.01
Forward intensity I(0) i030228000.00
Molecular weight molecular_weight42210.0 kDa
Excluded volume excluded_volume53020 ų
Envelope volume envelope_volume71094 ų
Hydration-shell volume shell_volume24066 ų
Envelope diameter envelope_diameter110.2
Shell Rg shell_rg31.44
Envelope Rg envelope_rg26.87
Shape Rg shape_rg25.97
Total Rg total_rg26.77
Total atoms total_atoms6020
Residues n_residues404
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 dmax102.4
Rg (real space) rg_real26.58
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real3.0230e+07
I(0) uncertainty (real space) i0_real_error5.5410e+05
Rg (reciprocal space) rg_reciprocal26.51
I(0) (reciprocal space) i0_reciprocal30230000.0000
Solution quality estimate total_estimate0.7599
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.584
Kurtosis Kurtosis kurtosis-0.060
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9091000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.489; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.432; Smooth: 0.976

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)