9qux

Solution structure of the Homer1 EVH1 domain

Method: SOLUTION NMR Dmax: 53.8 Å Quality: GOOD

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

Homer protein homolog 1

Mus musculus

UniProt Q9Z2Y3

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 1–118 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.36;298 K;Ionic strength (raw mmCIF value) 215;Pressure 1 NMR sample composition:180 uM [U-13C; U-15N] Homer1 EVH1, 50 mM Sodium phosphate buffer, 20 mM sodium chloride, 0.02 % NaN3, 95% H2O/5% D2O | 95% H2O/5% D2O Resolution not provided

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 HOME1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–121; UniProt 1–118

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 9qux

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9qux
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9qux
Deposition date deposition_date2025-04-11
Structure title titleSolution structure of the Homer1 EVH1 domain
Keywords keywordsPostsynapse, Enabled/VASP homology 1 domain, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.60
Radius of gyration Rg (electron density) rg_electron15.03
Forward intensity I(0) i01058770000.00
Molecular weight molecular_weight274850.0 kDa
Excluded volume excluded_volume343210 ų
Envelope volume envelope_volume34693 ų
Hydration-shell volume shell_volume16505 ų
Envelope diameter envelope_diameter61.4
Shell Rg shell_rg24.00
Envelope Rg envelope_rg18.82
Shape Rg shape_rg14.96
Total Rg total_rg15.44
Total atoms total_atoms38420
Residues n_residues2420
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 dmax53.8
Rg (real space) rg_real15.58
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real1.0590e+09
I(0) uncertainty (real space) i0_real_error1.1150e+07
Rg (reciprocal space) rg_reciprocal15.58
I(0) (reciprocal space) i0_reciprocal1059000000.0000
Solution quality estimate total_estimate0.8642
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.4
Skewness Skewness skewness0.295
Kurtosis Kurtosis kurtosis-0.183
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha316300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.752; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)