1sol

A PIP2 AND F-ACTIN-BINDING SITE OF GELSOLIN, RESIDUE 150-169 (NMR, AVERAGED STRUCTURE)

Method: SOLUTION NMR Dmax: 38.2 Å Quality: GOOD

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

GELSOLIN (150-169)

OrganismNot specified

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 177–196 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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.

60 other PDB entries and 94 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 1–20; UniProt 177–196

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 1sol

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1sol
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1sol
Deposition date deposition_date1995-09-29
Structure title titleA PIP2 AND F-ACTIN-BINDING SITE OF GELSOLIN, RESIDUE 150-169 (NMR, AVERAGED STRUCTURE)
Keywords keywordsACTIN-BINDING PROTEIN; ACTIN-BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier10.98
Radius of gyration Rg (electron density) rg_electron9.89
Forward intensity I(0) i0182872.00
Molecular weight molecular_weight2393.0 kDa
Excluded volume excluded_volume3045 ų
Envelope volume envelope_volume3929 ų
Hydration-shell volume shell_volume4169 ų
Envelope diameter envelope_diameter34.3
Shell Rg shell_rg13.47
Envelope Rg envelope_rg10.19
Shape Rg shape_rg9.85
Total Rg total_rg11.41
Total atoms total_atoms353
Residues n_residues20
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 dmax38.2
Rg (real space) rg_real11.10
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real1.8290e+05
I(0) uncertainty (real space) i0_real_error2.1120e+03
Rg (reciprocal space) rg_reciprocal11.10
I(0) (reciprocal space) i0_reciprocal182900.0000
Solution quality estimate total_estimate0.8452
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary11.1
Skewness Skewness skewness0.477
Kurtosis Kurtosis kurtosis-0.359
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21950.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.793; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.636; Smooth: 0.967

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1sola_
Class classj — Peptides
Fold Fold foldj.43 — Gelsolin fragment (residues 150-169)
Superfamily Superfamily superfamilyj.43.1 — Gelsolin fragment (residues 150-169)
Family Family familyj.43.1.1 — Gelsolin fragment (residues 150-169)

8. Citations (2)

9. Files and Curves (10)