8atm

Structure of the giant inhibitor of apoptosis, BIRC6 (composite map)

Method: ELECTRON MICROSCOPY Dmax: 195.6 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–4857 Chain B; UniProt 1–4857 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 3–4859; UniProt 1–4857 Author chain B; PDBConstruct 3–4859; UniProt 1–4857

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 8atm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8atm
Deposition date deposition_date2022-08-23
Structure title titleStructure of the giant inhibitor of apoptosis, BIRC6 (composite map)
Keywords keywordsE2/E3 ubiquitin ligase, APOPTOSIS; APOPTOSIS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier68.59
Radius of gyration Rg (electron density) rg_electron68.84
Forward intensity I(0) i02539260000.00
Molecular weight molecular_weight440470.0 kDa
Excluded volume excluded_volume558110 ų
Envelope volume envelope_volume955670 ų
Hydration-shell volume shell_volume117820 ų
Envelope diameter envelope_diameter212.8
Shell Rg shell_rg67.43
Envelope Rg envelope_rg65.42
Shape Rg shape_rg68.82
Total Rg total_rg68.88
Total atoms total_atoms30885
Residues n_residues3998
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 dmax195.6
Rg (real space) rg_real68.65
Rg uncertainty (real space) rg_real_error1.53
I(0) (real space) i0_real2.5390e+09
I(0) uncertainty (real space) i0_real_error5.8210e+07
Rg (reciprocal space) rg_reciprocal68.19
I(0) (reciprocal space) i0_reciprocal2537000000.0000
Solution quality estimate total_estimate0.8417
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.0
Skewness Skewness skewness0.217
Kurtosis Kurtosis kurtosis-0.873
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha118000000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.986; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)