9d58

Human Dystrophin tandem calponin homology actin-binding domain crystallized in a closed-state conformation

Method: X-RAY DIFFRACTION Dmax: 102.0 Å Quality: EXCELLENT

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

Dystrophin

Homo sapiens

UniProt P11532

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 2–246 Fragment:actin-binding domain/calponin homology domains 1 and 2 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M Bis-Tris pH 6.7, 30% w/v Polyethylene monomethyl ether (MPEG) 5,000 Resolution 1.94 Å R-free 0.262
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2–246 Fragment:actin-binding domain/calponin homology domains 1 and 2 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M Bis-Tris pH 6.7, 30% w/v Polyethylene monomethyl ether (MPEG) 5,000 Resolution 1.94 Å R-free 0.262
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 2–246 Fragment:actin-binding domain/calponin homology domains 1 and 2 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M Bis-Tris pH 6.7, 30% w/v Polyethylene monomethyl ether (MPEG) 5,000 Resolution 1.94 Å R-free 0.262
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 2–246 Fragment:actin-binding domain/calponin homology domains 1 and 2 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M Bis-Tris pH 6.7, 30% w/v Polyethylene monomethyl ether (MPEG) 5,000 Resolution 1.94 Å R-free 0.262

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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DMD_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–248; UniProt 2–246 Author chain B; PDBConstruct 4–248; UniProt 2–246 Author chain C; PDBConstruct 4–248; UniProt 2–246 Author chain D; PDBConstruct 4–248; UniProt 2–246

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 9d58

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9d58
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9d58
Deposition date deposition_date2024-08-13
最后修订 last_revision2025-03-12
Structure title titleHuman Dystrophin tandem calponin homology actin-binding domain crystallized in a closed-state conformation
Keywords keywords;Actin-binding domain, tandem calponin homology domain, Dystrophin, Duchenne Muscular Dystrophy, DMD, Cytoskeleton, 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_guinier33.74
Radius of gyration Rg (electron density) rg_electron32.62
Forward intensity I(0) i0160157000.00
Molecular weight molecular_weight102170.0 kDa
Excluded volume excluded_volume128530 ų
Envelope volume envelope_volume168810 ų
Hydration-shell volume shell_volume42943 ų
Envelope diameter envelope_diameter110.0
Shell Rg shell_rg39.77
Envelope Rg envelope_rg31.68
Shape Rg shape_rg32.63
Total Rg total_rg33.17
Total atoms total_atoms7230
Residues n_residues926
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 dmax102.0
Rg (real space) rg_real33.55
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real1.6020e+08
I(0) uncertainty (real space) i0_real_error2.5150e+06
Rg (reciprocal space) rg_reciprocal33.67
I(0) (reciprocal space) i0_reciprocal160200000.0000
Solution quality estimate total_estimate0.9054
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.8
Skewness Skewness skewness0.053
Kurtosis Kurtosis kurtosis-0.543
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29250000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.942

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)