SAXSdb — 2hd7

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

Twinfilin-1

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 176–316	Fragment：C-terminal domain, residues 176-316	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 6.8；298 K；Ionic strength (raw mmCIF value) 60；Pressure ambient NMR sample composition：1 mM C-terminal domain of twinfilin U-15N, C13, 10 mM Bis-Tris, pH 6.8, 50 mM NaCl, 1 mM DTT, 90% H2O, 10% D2O \| 90% H2O/10% 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 2HD7	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1M4J CRYSTAL STRUCTURE OF THE N-TERMINAL ADF-H DOMAIN OF MOUSE TWINFILIN ISOFORM-1 Deposited 2002-07-03	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–142（142 aa） Fragment：N-terminal ADF-H Domain Chain B 1–142（142 aa） Fragment：N-terminal ADF-H Domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；1.6M Na-Citrate, 3% PEG 400, 0.1M Na-Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.60 Å R-free 0.251
1M4J CRYSTAL STRUCTURE OF THE N-TERMINAL ADF-H DOMAIN OF MOUSE TWINFILIN ISOFORM-1 Deposited 2002-07-03	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–142（142 aa） Fragment：N-terminal ADF-H Domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；1.6M Na-Citrate, 3% PEG 400, 0.1M Na-Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.60 Å R-free 0.251
2D8B Solution structure of the second tandem cofilin-domain of mouse twinfilin Deposited 2005-12-02	Different construct Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 161–313（153 aa） Fragment：COFILIN HOMOLOGY DOMAIN, UNP Residues 161-313	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 1.44mM COFILIN HOMOLOGY DOMAIN, 20mM d-Tris-HCL, 100mM NaCl, 1mM d-DTT, 0.02 % NaN3; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
3DAW Structure of the actin-depolymerizing factor homology domain in complex with actin Deposited 2008-05-30	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 × 2 PDB declaration: dimeric	Chain B 167–322（156 aa） Fragment：C-terminal domain, ADF-H 2, UNP RESIDUES 167-322	Mutation：V168M	CA CALCIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；10mM Tris pH 7.5, 50mM NaCl, 0.2mM ATP, 0.2mM DTT, 0.2mM CaCl2, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.55 Å R-free 0.279
6RSW HFD domain of mouse CAP1 bound to the pointed end of G-actin Deposited 2019-05-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 176–316（141 aa）	Not recorded	MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；0.1M HEPES, 0.1 mM KCl, 10% PEG4000 (w/v)	Resolution 1.95 Å R-free 0.194
6YP9 Rabbit muscle actin in complex with ADF-H and ATP-ATTO-488 Deposited 2020-04-15	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 176–315（140 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；0.1 M sodium cacodylate (pH 6.0) and 15% (w/v) PEG 4000	Resolution 2.56 Å R-free 0.230
7DS2 Crystal structure of actin capping protein in complex with twinflin-1 C-terminus tail Deposited 2020-12-30	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 315–350（36 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；22.5% (w/v) PEG 400, 0.1M HEPES-NaOH (pH = 7.0)	Resolution 1.95 Å R-free 0.183
7DS4 Crystal structure of actin capping protein in complex with twinflin-1 C-terminus tail F323K mutant Deposited 2020-12-30	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 315–344（30 aa）	Mutation：F323K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；5% (w/v) PEG 3350, 5% (v/v) ethanol, 50mM Tris-HCl (pH = 7.0)	Resolution 1.85 Å R-free 0.259
7DS6 Crystal structure of actin capping protein in complex with twinflin-1/CD2AP CPI chimera peptide (TWN-CDC) Deposited 2020-12-30	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 315–327（13 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；5% (w/v) PEG 3350, 5% (v/v) ethanol, 50mM Tris-HCl (pH = 7.0)	Resolution 1.69 Å R-free 0.253
7DS8 Crystal structure of actin capping protein in complex with twinflin-1/CD2AP CPI chimera peptide (CDN-TWC) Deposited 2020-12-30	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 326–344（19 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；4% (w/v) PEG 3350, 50mM Tris-HCl (pH = 7.0)	Resolution 1.95 Å R-free 0.233
7DSB Crystal structure of actin capping protein in complex with V-1 and twinfilin C-terminal tail Deposited 2020-12-30	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 315–344（30 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；10% (w/v) PEG 3350, 5% (v/v) isopropanol, 0.1M HEPES-NaOH (pH = 7.5)	Resolution 2.44 Å R-free 0.248

10 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TWF1_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–142； UniProt 176–316

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	2hd7
Deposition date deposition_date	2006-06-20
Structure title title	Solution structure of C-teminal domain of twinfilin-1.
Keywords keywords	ADF-H, Actin binding protein, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
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	15.87 Å
Radius of gyration Rg (electron density) rg_electron	15.25 Å
Forward intensity I(0) i0	836525000.00
Molecular weight molecular_weight	249180.0 kDa
Excluded volume excluded_volume	313380 Å³
Envelope volume envelope_volume	33509 Å³
Hydration-shell volume shell_volume	16667 Å³
Envelope diameter envelope_diameter	56.8 Å
Shell Rg shell_rg	23.00 Å
Envelope Rg envelope_rg	17.28 Å
Shape Rg shape_rg	15.22 Å
Total Rg total_rg	15.48 Å
Total atoms total_atoms	35025
Residues n_residues	2130
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	53.8 Å
Rg (real space) rg_real	15.78 Å
Rg uncertainty (real space) rg_real_error	0.34 Å
I(0) (real space) i0_real	8.3650e+08
I(0) uncertainty (real space) i0_real_error	8.6040e+06
Rg (reciprocal space) rg_reciprocal	15.79 Å
I(0) (reciprocal space) i0_reciprocal	836500000.0000
Solution quality estimate total_estimate	0.8647
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	21.1 Å
Skewness Skewness skewness	0.138
Kurtosis Kurtosis kurtosis	-0.286
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	516300.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.747; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.997

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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) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2hd7a1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.109 — Gelsolin-like
Superfamily Superfamily superfamily	d.109.1 — Actin depolymerizing proteins
Family Family family	d.109.1.0 — automated matches

Domain ID domain_id	d2hd7a2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id	2hd7A00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	20 — Severin
Homologous superfamily homologous superfamily	10 — Severin

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	Twinfilin-1
Molecular weight formula_weight	16639.0 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	35025

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 BL21(DE3)

Solution structure of C-teminal domain of twinfilin-1.

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

Twinfilin-1

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/hd/2hd7/2hd7.fit
pddf	/app/data/pr_computation/hd/2hd7/2hd7.pr.out
profile	/app/data/saxs_computation/hd/2hd7/2hd7.dat