7p2b

Crystal structure of human gelsolin amyloid mutant A551P

Method: X-RAY DIFFRACTION Dmax: 175.7 Å Quality: REASONABLE

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

Gelsolin

Homo sapiens

UniProt P06396

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 28–782 Mutation:A551P SO4 SULFATE ION × 4 GOL GLYCEROL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;15% glycerol, 2.0 M ammonium sulfate, 0.1M tris HCl, pH8.5 Resolution 3.00 Å R-free 0.263
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 28–782 Mutation:A551P SO4 SULFATE ION × 3 GOL GLYCEROL × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;15% glycerol, 2.0 M ammonium sulfate, 0.1M tris HCl, pH8.5 Resolution 3.00 Å R-free 0.263

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.

60 other PDB entries and 93 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GELS_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 24–778; UniProt 28–782 Author chain B; PDBConstruct 24–778; UniProt 28–782

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 7p2b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7p2b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7p2b
Deposition date deposition_date2021-07-05
Structure title titleCrystal structure of human gelsolin amyloid mutant A551P
Keywords keywordsGelsolin protein, actin binding protein, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier47.98
Radius of gyration Rg (electron density) rg_electron49.09
Forward intensity I(0) i0386443000.00
Molecular weight molecular_weight159140.0 kDa
Excluded volume excluded_volume197830 ų
Envelope volume envelope_volume271790 ų
Hydration-shell volume shell_volume50961 ų
Envelope diameter envelope_diameter179.9
Shell Rg shell_rg46.44
Envelope Rg envelope_rg49.05
Shape Rg shape_rg49.10
Total Rg total_rg48.94
Total atoms total_atoms11219
Residues n_residues1426
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 dmax175.7
Rg (real space) rg_real48.93
Rg uncertainty (real space) rg_real_error2.19
I(0) (real space) i0_real3.8640e+08
I(0) uncertainty (real space) i0_real_error7.4480e+06
Rg (reciprocal space) rg_reciprocal47.99
I(0) (reciprocal space) i0_reciprocal386000000.0000
Solution quality estimate total_estimate0.7129
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.3
Skewness Skewness skewness0.624
Kurtosis Kurtosis kurtosis-0.364
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha42510000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.394; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.432; Smooth: 0.648

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)