6ei6

CC2D1B coordinates ESRCT-III activity during the mitotic reformation of the nuclear envelope

Method: X-RAY DIFFRACTION Dmax: 125.8 Å Quality: GOOD

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

Coiled-coil and C2 domain-containing protein 1-like

Drosophila melanogaster

UniProt Q9VKJ9

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 550–816 Not recorded SO4 SULFATE ION × 3 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;290 K;0.1 M Bis-Tris pH 6.5, 15-25% PEG 3500 Mme, 200 mM ammonium sulfate Resolution 2.46 Å R-free 0.247
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 550–816 Not recorded SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;290 K;0.1 M Bis-Tris pH 6.5, 15-25% PEG 3500 Mme, 200 mM ammonium sulfate Resolution 2.46 Å R-free 0.247

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.

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C2D1_DROME
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–270; UniProt 550–816 Author chain B; PDBConstruct 4–270; UniProt 550–816

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 6ei6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ei6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ei6
Deposition date deposition_date2017-09-18
Structure title titleCC2D1B coordinates ESRCT-III activity during the mitotic reformation of the nuclear envelope
Keywords keywordsESCRT protein regulator, nuclear envelope reformation, polymerization, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.24
Radius of gyration Rg (electron density) rg_electron36.32
Forward intensity I(0) i055369700.00
Molecular weight molecular_weight57269.0 kDa
Excluded volume excluded_volume70938 ų
Envelope volume envelope_volume102390 ų
Hydration-shell volume shell_volume25565 ų
Envelope diameter envelope_diameter131.0
Shell Rg shell_rg39.18
Envelope Rg envelope_rg35.57
Shape Rg shape_rg36.37
Total Rg total_rg36.36
Total atoms total_atoms4005
Residues n_residues484
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 dmax125.8
Rg (real space) rg_real36.68
Rg uncertainty (real space) rg_real_error1.82
I(0) (real space) i0_real5.5370e+07
I(0) uncertainty (real space) i0_real_error1.1010e+06
Rg (reciprocal space) rg_reciprocal36.41
I(0) (reciprocal space) i0_reciprocal55360000.0000
Solution quality estimate total_estimate0.7614
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.7
Skewness Skewness skewness0.451
Kurtosis Kurtosis kurtosis-0.649
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3802000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.603; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.346; Smooth: 0.739

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)