SAXSdb — 2adz

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

Alpha-1-syntrophin

Mus musculus

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 2–79 Chain A； UniProt 165–264	Fragment：PH domain	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 7；303 K；Pressure ambient NMR sample composition：1mM protein 15N; 100mM potassium phosphate pH 7.0 \| 90% H2O/10% D2O NMR sample composition：1mM protein 15N, 13C; 100mM potassium phosphate pH 7.0 \| 99.9% D2O NMR sample composition：1mM unlabelled protein; 100mM potassium phosphate pH 7.0 \| 99.9% 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.

Other PDB	Difference from Current Entry 2ADZ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1QAV Unexpected Modes of PDZ Domain Scaffolding Revealed by Structure of NNOS-Syntrophin Complex Deposited 1999-03-30	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 75–164（90 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；VAPOR DIFFUSION, SITTING DROP, PH 8.5, 298K, 25% PEG4000, 0.2M SODIUM ACETATE, 100MM TRIS	Resolution 1.90 Å R-free 0.259
1Z86 Solution structure of the PDZ domain of alpha-syntrophin Deposited 2005-03-30	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 79–165（87 aa） Fragment：PDZ domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；303 K；Pressure ambient NMR sample composition 1mM PDZ domain of alpha1-syntrophin U-15N, 13C; 100mM potassium phosphate; 90% H2O,10% D2O \| 90% H2O/10% D2O NMR sample composition 1mM PDZ domain of alpha1-syntrophin U-15N; 100mM potassium phosphate; 90% H2O,10% D2O \| 90% H2O/10% D2O NMR sample composition 1mM PDZ domain of alpha1-syntrophin U-15N, 13C; 100mM potassium phosphate; 99.9% D2O \| 99.9% D2O NMR sample composition 1mM PDZ domain of alpha1-syntrophin; 100mM potassium phosphate; 99.9% D2O \| 99.9% D2O	Resolution not provided
1Z87 solution structure of the split PH-PDZ Supramodule of alpha-Syntrophin Deposited 2005-03-30	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–264（263 aa） Fragment：the PHN-PDZ-PHC tandem	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；303 K；Pressure ambient NMR sample composition 1mM PHN-PDZ-PHC tandem of alpha1-syntrophin U-15N, 13C; 100mM potassium phosphate; 90% H2O,10% D2O \| 90% H2O/10% D2O NMR sample composition 1mM PHN-PDZ-PHC tandem of alpha1-syntrophin U-15N; 100mM potassium phosphate; 90% H2O,10% D2O \| 90% H2O/10% D2O NMR sample composition 1mM PHN-PDZ-PHC tandem of alpha1-syntrophin U-15N, 13C; 100mM potassium phosphate; 99.9% D2O \| 99.9% D2O NMR sample composition 1mM PHN-PDZ-PHC tandem of alpha1-syntrophin; 100mM potassium phosphate; 99.9% D2O \| 99.9% D2O	Resolution not provided
2PDZ SOLUTION STRUCTURE OF THE SYNTROPHIN PDZ DOMAIN IN COMPLEX WITH THE PEPTIDE GVKESLV, NMR, 15 STRUCTURES Deposited 1997-12-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 79–164（86 aa） Fragment：PDZ DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.2；295 K；Ionic strength (raw mmCIF value) 70mM；Pressure 1 NMR sample composition H2O	Resolution not provided
4HOP Crystal structure of the computationally designed NNOS-Syntrophin complex Deposited 2012-10-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 77–162（86 aa） Fragment：PDZ DOMAIN (RESIDUES 77-162)	Mutation：H142F	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.25；293 K；0.1M MES, 0.2M LICL, 21.5% PEG 6000. SYNTROPHIN AT 3.6 MG/ML FINAL. NNOS AT 2.6 MG/ML FINAL. 1:1 MIX OF PROTEIN SOLUTION TO PRECIPITANT, pH 5.25, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.29 Å R-free 0.273
4HOP Crystal structure of the computationally designed NNOS-Syntrophin complex Deposited 2012-10-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 77–162（86 aa） Fragment：PDZ DOMAIN (RESIDUES 77-162)	Mutation：H142F	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.25；293 K；0.1M MES, 0.2M LICL, 21.5% PEG 6000. SYNTROPHIN AT 3.6 MG/ML FINAL. NNOS AT 2.6 MG/ML FINAL. 1:1 MIX OF PROTEIN SOLUTION TO PRECIPITANT, pH 5.25, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.29 Å R-free 0.273
4HOP Crystal structure of the computationally designed NNOS-Syntrophin complex Deposited 2012-10-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 77–162（86 aa） Fragment：PDZ DOMAIN (RESIDUES 77-162)	Mutation：H142F	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.25；293 K；0.1M MES, 0.2M LICL, 21.5% PEG 6000. SYNTROPHIN AT 3.6 MG/ML FINAL. NNOS AT 2.6 MG/ML FINAL. 1:1 MIX OF PROTEIN SOLUTION TO PRECIPITANT, pH 5.25, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.29 Å R-free 0.273

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	SNTA1_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–78； UniProt 2–79 Author chain A； PDBConstruct 79–178； UniProt 165–264

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2adz
Deposition date deposition_date	2005-07-21
Structure title title	solution structure of the joined PH domain of alpha1-syntrophin
Keywords keywords	PROTEIN BINDING; PROTEIN BINDING
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	21.51 Å
Radius of gyration Rg (electron density) rg_electron	21.11 Å
Forward intensity I(0) i0	2170120000.00
Molecular weight molecular_weight	372300.0 kDa
Excluded volume excluded_volume	458080 Å³
Envelope volume envelope_volume	121870 Å³
Hydration-shell volume shell_volume	36276 Å³
Envelope diameter envelope_diameter	85.9 Å
Shell Rg shell_rg	35.48 Å
Envelope Rg envelope_rg	28.08 Å
Shape Rg shape_rg	21.12 Å
Total Rg total_rg	21.42 Å
Total atoms total_atoms	51860
Residues n_residues	3560
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	80.9 Å
Rg (real space) rg_real	21.59 Å
Rg uncertainty (real space) rg_real_error	0.61 Å
I(0) (real space) i0_real	2.1700e+09
I(0) uncertainty (real space) i0_real_error	3.0610e+07
Rg (reciprocal space) rg_reciprocal	21.58 Å
I(0) (reciprocal space) i0_reciprocal	2170000000.0000
Solution quality estimate total_estimate	0.7364
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	22.6 Å
Skewness Skewness skewness	0.440
Kurtosis Kurtosis kurtosis	-0.246
Angular range angular_range	— – 0.3700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2367000.0000
Real-space data points n_real_points	69
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.626; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.690; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d2adza1
Class class	b — All beta proteins
Fold Fold fold	b.55 — PH domain-like barrel
Superfamily Superfamily superfamily	b.55.1 — PH domain-like
Family Family family	b.55.1.1 — Pleckstrin-homology domain (PH domain)

CATH v4.4 (1 domains)

Domain ID domain_id	2adzA01
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	29 — PH-domain like
Homologous superfamily homologous superfamily	30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

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8. Citations (1)

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Description description	Alpha-1-syntrophin
Molecular weight formula_weight	18635.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	51860

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

fit	/app/data/saxs_computation/ad/2adz/2adz.fit
pddf	/app/data/pr_computation/ad/2adz/2adz.pr.out
profile	/app/data/saxs_computation/ad/2adz/2adz.dat

solution structure of the joined PH domain of alpha1-syntrophin

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

Alpha-1-syntrophin

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)