8e2h

Cryo-EM structure of C-terminal arm of BIRC6 (from local refinement 4)

Method: ELECTRON MICROSCOPY Dmax: 114.4 Å Quality: REASONABLE

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–4857 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.30 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 32–4888; 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 8e2h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8e2h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8e2h
Deposition date deposition_date2022-08-15
Structure title titleCryo-EM structure of C-terminal arm of BIRC6 (from local refinement 4)
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_guinier32.90
Radius of gyration Rg (electron density) rg_electron32.84
Forward intensity I(0) i076044600.00
Molecular weight molecular_weight72596.0 kDa
Excluded volume excluded_volume92473 ų
Envelope volume envelope_volume116230 ų
Hydration-shell volume shell_volume31577 ų
Envelope diameter envelope_diameter113.5
Shell Rg shell_rg36.79
Envelope Rg envelope_rg33.02
Shape Rg shape_rg32.83
Total Rg total_rg33.23
Total atoms total_atoms10372
Residues n_residues656
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 dmax114.4
Rg (real space) rg_real33.31
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real7.6040e+07
I(0) uncertainty (real space) i0_real_error1.4390e+06
Rg (reciprocal space) rg_reciprocal33.14
I(0) (reciprocal space) i0_reciprocal76030000.0000
Solution quality estimate total_estimate0.5951
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.547
Kurtosis Kurtosis kurtosis-0.402
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha14800000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.697; Stabil: 1.000; Sysdev: 0.049; Positv: 1.000; Valcen: 0.641; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)