8e2k

Cryo-EM structure of BIRC6/HtrA2-S306A

Method: ELECTRON MICROSCOPY Dmax: 232.2 Å Quality: GOOD

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

Baculoviral IAP repeat-containing protein 6

Homo sapiens

UniProt Q9NR09

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–4857 Chain B; UniProt 1–4857 Not recorded Serine protease HTRA2, mitochondrial × 3 (O43464) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.21 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.

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

View Construct and Data Evidence
UniProt name BIRC6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 42–4898; UniProt 1–4857 Author chain B; PDBConstruct 42–4898; UniProt 1–4857

Serine protease HTRA2, mitochondrial

Homo sapiens

UniProt O43464

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain X; UniProt 134–458 Chain Y; UniProt 134–458 Chain Z; UniProt 134–458 Not recorded Baculoviral IAP repeat-containing protein 6 × 2 (Q9NR09) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.21 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.

12 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HTRA2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain X; PDBConstruct 2–326; UniProt 134–458 Author chain Y; PDBConstruct 2–326; UniProt 134–458 Author chain Z; PDBConstruct 2–326; UniProt 134–458

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 8e2k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8e2k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8e2k
Deposition date deposition_date2022-08-15
Structure title titleCryo-EM structure of BIRC6/HtrA2-S306A
Keywords keywordsUbiquitin, E3 ligase, Apoptosis, Autophagy, IAP, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier71.43
Radius of gyration Rg (electron density) rg_electron71.55
Forward intensity I(0) i06047490000.00
Molecular weight molecular_weight680210.0 kDa
Excluded volume excluded_volume860690 ų
Envelope volume envelope_volume1356300 ų
Hydration-shell volume shell_volume156820 ų
Envelope diameter envelope_diameter217.0
Shell Rg shell_rg72.07
Envelope Rg envelope_rg68.15
Shape Rg shape_rg71.52
Total Rg total_rg71.69
Total atoms total_atoms96469
Residues n_residues6160
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 dmax232.2
Rg (real space) rg_real71.24
Rg uncertainty (real space) rg_real_error1.98
I(0) (real space) i0_real6.0480e+09
I(0) uncertainty (real space) i0_real_error1.4330e+08
Rg (reciprocal space) rg_reciprocal71.91
I(0) (reciprocal space) i0_reciprocal6054000000.0000
Solution quality estimate total_estimate0.8728
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary84.4
Skewness Skewness skewness0.086
Kurtosis Kurtosis kurtosis-0.730
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha246800000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.577

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)