8d9x

Cryo-EM structure of human DELE1 in oligomeric form

Method: ELECTRON MICROSCOPY Dmax: 143.4 Å Quality: GOOD

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

Maltodextrin-binding protein,DAP3-binding cell death enhancer 1 short form

Homo sapiens

UniProt A0A376KDN7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 27–387 Chain B; UniProt 27–387 Chain C; UniProt 27–387 Chain D; UniProt 27–387 Chain E; UniProt 27–387 Chain F; UniProt 27–387 Chain G; UniProt 27–387 Chain H; UniProt 27–387 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

19 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A376KDN7_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–362; UniProt 27–387 Author chain B; PDBConstruct 2–362; UniProt 27–387 Author chain C; PDBConstruct 2–362; UniProt 27–387 Author chain D; PDBConstruct 2–362; UniProt 27–387 Author chain E; PDBConstruct 2–362; UniProt 27–387 Author chain F; PDBConstruct 2–362; UniProt 27–387 Author chain G; PDBConstruct 2–362; UniProt 27–387 Author chain H; PDBConstruct 2–362; UniProt 27–387

Maltodextrin-binding protein,DAP3-binding cell death enhancer 1 short form

Homo sapiens

UniProt Q14154

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 224–515 Chain B; UniProt 224–515 Chain C; UniProt 224–515 Chain D; UniProt 224–515 Chain E; UniProt 224–515 Chain F; UniProt 224–515 Chain G; UniProt 224–515 Chain H; UniProt 224–515 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name DELE1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 372–663; UniProt 224–515 Author chain B; PDBConstruct 372–663; UniProt 224–515 Author chain C; PDBConstruct 372–663; UniProt 224–515 Author chain D; PDBConstruct 372–663; UniProt 224–515 Author chain E; PDBConstruct 372–663; UniProt 224–515 Author chain F; PDBConstruct 372–663; UniProt 224–515 Author chain G; PDBConstruct 372–663; UniProt 224–515 Author chain H; PDBConstruct 372–663; UniProt 224–515

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 8d9x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8d9x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8d9x
Deposition date deposition_date2022-06-11
Structure title titleCryo-EM structure of human DELE1 in oligomeric form
Keywords keywordsOligomer, Mitochondria, Integrated Stress Response, Kinase, Tetratricopeptide repeat, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.77
Radius of gyration Rg (electron density) rg_electron44.05
Forward intensity I(0) i0511957000.00
Molecular weight molecular_weight179630.0 kDa
Excluded volume excluded_volume222580 ų
Envelope volume envelope_volume346380 ų
Hydration-shell volume shell_volume68403 ų
Envelope diameter envelope_diameter151.9
Shell Rg shell_rg46.97
Envelope Rg envelope_rg42.45
Shape Rg shape_rg44.05
Total Rg total_rg44.18
Total atoms total_atoms12670
Residues n_residues1680
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 dmax143.4
Rg (real space) rg_real43.88
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real5.1200e+08
I(0) uncertainty (real space) i0_real_error9.1160e+06
Rg (reciprocal space) rg_reciprocal43.77
I(0) (reciprocal space) i0_reciprocal511900000.0000
Solution quality estimate total_estimate0.8297
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.8
Skewness Skewness skewness0.470
Kurtosis Kurtosis kurtosis-0.271
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha533300000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.719; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.628

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)