8wqi

Local refinement of FEM1B bound with the C-degron of CUX1

Method: ELECTRON MICROSCOPY Dmax: 100.1 Å Quality: GOOD

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

Protein fem-1 homolog B

Homo sapiens

UniProt Q9UK73

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–627 Not recorded Protein CASP × 1 (Q13948) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

30 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FEM1B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 1–627; UniProt 1–627

Protein CASP

Homo sapiens

UniProt Q13948

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 656–678 Not recorded Protein fem-1 homolog B × 1 (Q9UK73) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CASP_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 9–31; UniProt 656–678

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 8wqi

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8wqi
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8wqi
Deposition date deposition_date2023-10-11
Structure title titleLocal refinement of FEM1B bound with the C-degron of CUX1
Keywords keywordsE3 ubiquitin ligase, Pro/C-degron, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.27
Radius of gyration Rg (electron density) rg_electron32.03
Forward intensity I(0) i085518800.00
Molecular weight molecular_weight72213.0 kDa
Excluded volume excluded_volume89954 ų
Envelope volume envelope_volume118420 ų
Hydration-shell volume shell_volume31508 ų
Envelope diameter envelope_diameter104.0
Shell Rg shell_rg37.96
Envelope Rg envelope_rg31.98
Shape Rg shape_rg32.00
Total Rg total_rg32.62
Total atoms total_atoms5074
Residues n_residues644
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 dmax100.1
Rg (real space) rg_real32.28
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real8.5520e+07
I(0) uncertainty (real space) i0_real_error1.3580e+06
Rg (reciprocal space) rg_reciprocal32.28
I(0) (reciprocal space) i0_reciprocal85520000.0000
Solution quality estimate total_estimate0.8964
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.211
Kurtosis Kurtosis kurtosis-0.751
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16130000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.965; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.951; Smooth: 0.804

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)