8f21

Structure of a 30mer DegP cage bound to the client protein hTRF1

Method: ELECTRON MICROSCOPY Dmax: 120.9 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 × 90 PDB declaration: 90-meric(90) Consistent with protein copy count Chain A; UniProt 38–385 Chain B; UniProt 38–385 Chain C; UniProt 38–385 Chain D; UniProt 400–474 Chain E; UniProt 400–474 Chain F; UniProt 400–474 Fragment:protease and PDZ1 domains (UNP residues 38-385) Fragment:PDZ2 domain (UNP residues 400-474) Telomeric repeat-binding factor 1 × 30 (P54274) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 14.10 Å
2 Protein heterocomplex Heteromer Protein × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 38–385 Chain B; UniProt 38–385 Chain C; UniProt 38–385 Chain D; UniProt 400–474 Chain E; UniProt 400–474 Chain F; UniProt 400–474 Fragment:protease and PDZ1 domains (UNP residues 38-385) Fragment:PDZ2 domain (UNP residues 400-474) Telomeric repeat-binding factor 1 × 3 (P54274) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 14.10 Å
3 Protein heterocomplex Heteromer Protein × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 38–385 Chain B; UniProt 38–385 Chain C; UniProt 38–385 Chain D; UniProt 400–474 Chain E; UniProt 400–474 Chain F; UniProt 400–474 Fragment:protease and PDZ1 domains (UNP residues 38-385) Fragment:PDZ2 domain (UNP residues 400-474) Telomeric repeat-binding factor 1 × 3 (P54274) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 14.10 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 31 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 B; PDBConstruct 1–348; UniProt 38–385 Author chain C; PDBConstruct 1–348; UniProt 38–385 Author chain D; PDBConstruct 1–75; UniProt 400–474 Author chain E; PDBConstruct 1–75; UniProt 400–474 Author chain F; 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 × 90 PDB declaration: 90-meric(90) Consistent with protein copy count Chain a; UniProt 404–430 Chain b; UniProt 404–430 Chain c; UniProt 404–430 Fragment:UNP residues 404-430 Periplasmic serine endoprotease DegP × 30 (P0C0V0) Periplasmic serine endoprotease DegP × 30 (P0C0V0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 14.10 Å
2 Protein heterocomplex Heteromer Protein × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain a; UniProt 404–430 Chain b; UniProt 404–430 Chain c; UniProt 404–430 Fragment:UNP residues 404-430 Periplasmic serine endoprotease DegP × 3 (P0C0V0) Periplasmic serine endoprotease DegP × 3 (P0C0V0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 14.10 Å
3 Protein heterocomplex Heteromer Protein × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain a; UniProt 404–430 Chain b; UniProt 404–430 Chain c; UniProt 404–430 Fragment:UNP residues 404-430 Periplasmic serine endoprotease DegP × 3 (P0C0V0) Periplasmic serine endoprotease DegP × 3 (P0C0V0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 14.10 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 71 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 Author chain b; PDBConstruct 1–27; UniProt 404–430 Author chain c; 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 8f21

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8f21
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8f21
Deposition date deposition_date2022-11-06
Structure title titleStructure of a 30mer 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_guinier36.94
Radius of gyration Rg (electron density) rg_electron36.54
Forward intensity I(0) i0245616000.00
Molecular weight molecular_weight126630.0 kDa
Excluded volume excluded_volume159060 ų
Envelope volume envelope_volume214330 ų
Hydration-shell volume shell_volume49640 ų
Envelope diameter envelope_diameter123.8
Shell Rg shell_rg42.01
Envelope Rg envelope_rg36.82
Shape Rg shape_rg36.50
Total Rg total_rg37.06
Total atoms total_atoms18060
Residues n_residues1212
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 dmax120.9
Rg (real space) rg_real36.98
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real2.4560e+08
I(0) uncertainty (real space) i0_real_error4.1140e+06
Rg (reciprocal space) rg_reciprocal36.96
I(0) (reciprocal space) i0_reciprocal245600000.0000
Solution quality estimate total_estimate0.8871
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.2
Skewness Skewness skewness0.333
Kurtosis Kurtosis kurtosis-0.523
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha60160000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)