9duo

Human PELP1-WDR18 complex

Method: ELECTRON MICROSCOPY Dmax: 112.5 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 Proline-, glutamic acid- and leucine-rich protein 1 × 2 (Q8IZL8) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20mM Hepes pH8.0, 250mM NaCl, 5mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.66 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 3–434; UniProt 1–432 Author chain B; PDBConstruct 3–434; UniProt 1–432

Proline-, glutamic acid- and leucine-rich protein 1

Homo sapiens

UniProt Q8IZL8

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 1–642 Chain D; UniProt 1–642 Not recorded WD repeat-containing protein 18 × 2 (Q9BV38) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20mM Hepes pH8.0, 250mM NaCl, 5mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.66 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 PELP1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 3–644; UniProt 1–642 Author chain D; PDBConstruct 3–644; UniProt 1–642

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 9duo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9duo
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9duo
Deposition date deposition_date2024-10-03
Structure title titleHuman PELP1-WDR18 complex
Keywords keywordsComplex, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.19
Radius of gyration Rg (electron density) rg_electron36.32
Forward intensity I(0) i0522526000.00
Molecular weight molecular_weight188160.0 kDa
Excluded volume excluded_volume236720 ų
Envelope volume envelope_volume300830 ų
Hydration-shell volume shell_volume66593 ų
Envelope diameter envelope_diameter109.4
Shell Rg shell_rg44.99
Envelope Rg envelope_rg35.53
Shape Rg shape_rg36.33
Total Rg total_rg36.82
Total atoms total_atoms13187
Residues n_residues1736
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 dmax112.5
Rg (real space) rg_real36.93
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real5.2250e+08
I(0) uncertainty (real space) i0_real_error8.4240e+06
Rg (reciprocal space) rg_reciprocal37.10
I(0) (reciprocal space) i0_reciprocal522600000.0000
Solution quality estimate total_estimate0.8338
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.7
Skewness Skewness skewness0.073
Kurtosis Kurtosis kurtosis-0.609
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha106300000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)