8iw5

Crystal structure of liprin-beta H2H3 dimer

Method: X-RAY DIFFRACTION Dmax: 45.8 Å Quality: GOOD

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

Liprin-beta-1

Mus musculus

UniProt Q8C8U0

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 43–89 Chain B; UniProt 43–89 Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.05 M Calcium acetate, 0.1 M Sodium cacodylate pH 6.0 and 25% v/v MPD Resolution 1.70 Å R-free 0.272

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LIPB1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–51; UniProt 43–89 Author chain B; PDBConstruct 5–51; UniProt 43–89

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 8iw5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8iw5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8iw5
Deposition date deposition_date2023-03-29
Structure title titleCrystal structure of liprin-beta H2H3 dimer
Keywords keywordsFocal adhesion, Cortical microtubule stabilizing complex, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.21
Radius of gyration Rg (electron density) rg_electron12.49
Forward intensity I(0) i02380080.00
Molecular weight molecular_weight10271.0 kDa
Excluded volume excluded_volume12759 ų
Envelope volume envelope_volume14494 ų
Hydration-shell volume shell_volume10096 ų
Envelope diameter envelope_diameter45.7
Shell Rg shell_rg17.89
Envelope Rg envelope_rg12.74
Shape Rg shape_rg12.43
Total Rg total_rg13.92
Total atoms total_atoms714
Residues n_residues92
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 dmax45.8
Rg (real space) rg_real14.11
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real2.3800e+06
I(0) uncertainty (real space) i0_real_error2.3510e+04
Rg (reciprocal space) rg_reciprocal14.11
I(0) (reciprocal space) i0_reciprocal2380000.0000
Solution quality estimate total_estimate0.7946
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.6
Skewness Skewness skewness0.134
Kurtosis Kurtosis kurtosis-0.206
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha462300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.778; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)