SAXSdb — 1qag

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

UTROPHIN ACTIN BINDING REGION

Homo sapiens

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 31–256	Fragment：RESIDUES 28-261 Mutation：SELENOMETHIONINE REPLACES METHIONINE Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.5；293 K；0.1M Sodium Acetate pH 4.7, 2.0 M unbuffered sodium formate., pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.00 Å R-free 0.258
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 31–256	Fragment：RESIDUES 28-261 Mutation：SELENOMETHIONINE REPLACES METHIONINE Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.5；293 K；0.1M Sodium Acetate pH 4.7, 2.0 M unbuffered sodium formate., pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.00 Å R-free 0.258
3	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 31–256 Chain B； UniProt 31–256	Fragment：RESIDUES 28-261 Mutation：SELENOMETHIONINE REPLACES METHIONINE Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.5；293 K；0.1M Sodium Acetate pH 4.7, 2.0 M unbuffered sodium formate., pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.00 Å R-free 0.258

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 1QAG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BHD SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN Deposited 1998-06-05	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 144–261（118 aa） Fragment：2ND CALPONIN HOMOLOGY DOMAIN FROM ACTIN BINDING REGION	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.6；pH 7.6	Resolution 2.00 Å R-free 0.257
1BHD SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN Deposited 1998-06-05	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 144–261（118 aa） Fragment：2ND CALPONIN HOMOLOGY DOMAIN FROM ACTIN BINDING REGION	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.6；pH 7.6	Resolution 2.00 Å R-free 0.257
6M5G F-actin-Utrophin complex Deposited 2020-03-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain F 1–261（261 aa） Fragment：calponin domain 1, calponin domain 2 Chain G 1–261（261 aa） Fragment：calponin domain 1, calponin domain 2 Chain H 1–261（261 aa） Fragment：calponin domain 1, calponin domain 2	Not recorded	MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot for 3 seconds	Resolution 3.60 Å

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	UTRO_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–226； UniProt 31–256 Author chain B； PDBConstruct 1–226； UniProt 31–256

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	1qag
Deposition date deposition_date	1999-03-05
Structure title title	Actin binding region of the dystrophin homologue utrophin
Keywords keywords	CALPONIN HOMOLOGY DOMAIN, DOMAIN SWAPPING, ACTIN BINDING, UTROPHIN, DYSTROPHIN, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	28.48 Å
Radius of gyration Rg (electron density) rg_electron	27.56 Å
Forward intensity I(0) i0	43473000.00
Molecular weight molecular_weight	52105.0 kDa
Excluded volume excluded_volume	65602 Å³
Envelope volume envelope_volume	81154 Å³
Hydration-shell volume shell_volume	25528 Å³
Envelope diameter envelope_diameter	89.6 Å
Shell Rg shell_rg	33.64 Å
Envelope Rg envelope_rg	27.32 Å
Shape Rg shape_rg	27.57 Å
Total Rg total_rg	28.20 Å
Total atoms total_atoms	3642
Residues n_residues	442
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	89.7 Å
Rg (real space) rg_real	28.48 Å
Rg uncertainty (real space) rg_real_error	0.74 Å
I(0) (real space) i0_real	4.3470e+07
I(0) uncertainty (real space) i0_real_error	7.3040e+05
Rg (reciprocal space) rg_reciprocal	28.49 Å
I(0) (reciprocal space) i0_reciprocal	43470000.0000
Solution quality estimate total_estimate	0.8979
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	24.0 Å
Skewness Skewness skewness	0.208
Kurtosis Kurtosis kurtosis	-0.742
Angular range angular_range	— – 0.2800 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	11920000.0000
Real-space data points n_real_points	57
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.928; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.936; Smooth: 0.949

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1qaga1
Class class	a — All alpha proteins
Fold Fold fold	a.40 — CH domain-like
Superfamily Superfamily superfamily	a.40.1 — Calponin-homology domain, CH-domain
Family Family family	a.40.1.1 — Calponin-homology domain, CH-domain

Domain ID domain_id	d1qaga2
Class class	a — All alpha proteins
Fold Fold fold	a.40 — CH domain-like
Superfamily Superfamily superfamily	a.40.1 — Calponin-homology domain, CH-domain
Family Family family	a.40.1.1 — Calponin-homology domain, CH-domain

Domain ID domain_id	d1qagb1
Class class	a — All alpha proteins
Fold Fold fold	a.40 — CH domain-like
Superfamily Superfamily superfamily	a.40.1 — Calponin-homology domain, CH-domain
Family Family family	a.40.1.1 — Calponin-homology domain, CH-domain

Domain ID domain_id	d1qagb2
Class class	a — All alpha proteins
Fold Fold fold	a.40 — CH domain-like
Superfamily Superfamily superfamily	a.40.1 — Calponin-homology domain, CH-domain
Family Family family	a.40.1.1 — Calponin-homology domain, CH-domain

CATH v4.4 (4 domains)

Domain ID domain_id	1qagA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	10 — Calponin-like domain

Domain ID domain_id	1qagA02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	10 — Calponin-like domain

Domain ID domain_id	1qagB01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	10 — Calponin-like domain

Domain ID domain_id	1qagB02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily	10 — Calponin-like domain

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8. Citations (1)

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Unit-cell length a length_a	150.145 Å
Unit-cell length b length_b	55.160 Å
Unit-cell length c length_c	80.420 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	106.06 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	99.000 Å
R factor r_factor	—
R_work r_work	0.1980
R_free r_free	0.2580

Description description	UTROPHIN ACTIN BINDING REGION
Molecular weight formula_weight	26112.3 kDa
Mutation mutation	SELENOMETHIONINE REPLACES METHIONINE
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3654

Actin binding region of the dystrophin homologue utrophin

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

UTROPHIN ACTIN BINDING REGION

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

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	12

fit	/app/data/saxs_computation/qa/1qag/1qag.fit
pddf	/app/data/pr_computation/qa/1qag/1qag.pr.out
profile	/app/data/saxs_computation/qa/1qag/1qag.dat