7uwf

Human Rix1 sub-complex scaffold

Method: ELECTRON MICROSCOPY Dmax: 107.5 Å Quality: GOOD

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

WD repeat-containing protein 18

Homo sapiens

UniProt Q9BV38

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–432 Chain B; UniProt 1–432 Not recorded Modulator of non-genomic activity of estrogen receptor × 2 (C9JFV4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WDR18_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–432; UniProt 1–432 Author chain B; PDBConstruct 1–432; UniProt 1–432

Modulator of non-genomic activity of estrogen receptor

Homo sapiens

UniProt C9JFV4

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 51–692 Chain D; UniProt 51–692 Not recorded WD repeat-containing protein 18 × 2 (Q9BV38) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name C9JFV4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 11–652; UniProt 51–692 Author chain D; PDBConstruct 11–652; UniProt 51–692

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 7uwf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7uwf
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7uwf
Deposition date deposition_date2022-05-03
Structure title titleHuman Rix1 sub-complex scaffold
Keywords keywordsscaffold, complex, WD-repeat, solenoid, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.09
Radius of gyration Rg (electron density) rg_electron36.23
Forward intensity I(0) i0517361000.00
Molecular weight molecular_weight188370.0 kDa
Excluded volume excluded_volume237450 ų
Envelope volume envelope_volume300810 ų
Hydration-shell volume shell_volume66673 ų
Envelope diameter envelope_diameter108.4
Shell Rg shell_rg44.93
Envelope Rg envelope_rg35.40
Shape Rg shape_rg36.24
Total Rg total_rg36.74
Total atoms total_atoms13168
Residues n_residues1754
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 dmax107.5
Rg (real space) rg_real36.82
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real5.1740e+08
I(0) uncertainty (real space) i0_real_error7.5670e+06
Rg (reciprocal space) rg_reciprocal36.99
I(0) (reciprocal space) i0_reciprocal517400000.0000
Solution quality estimate total_estimate0.8914
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.0
Skewness Skewness skewness0.064
Kurtosis Kurtosis kurtosis-0.603
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha113600000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.979; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.671

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)