SAXSdb — 2f31

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

Diaphanous protein homolog 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 135–367 Chain B； UniProt 1177–1196	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；0.1 M sodium citrate, 200 mM ammonium sulfate, 25% PEG 4000, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.10 Å R-free 0.312
2	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 135–367 Chain B； UniProt 1177–1196	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；0.1 M sodium citrate, 200 mM ammonium sulfate, 25% PEG 4000, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.10 Å R-free 0.312

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 2F31	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1V9D Crystal structure of the core FH2 domain of mouse mDia1 Deposited 2004-01-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 826–1163（338 aa） Fragment：core FH2 domain Chain B 826–1163（338 aa） Fragment：core FH2 domain Chain C 826–1163（338 aa） Fragment：core FH2 domain Chain D 826–1163（338 aa） Fragment：core FH2 domain	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.3；293 K；PEG3350, sodium sulfate, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K	Resolution 2.60 Å R-free 0.267
1Z2C Crystal structure of mDIA1 GBD-FH3 in complex with RhoC-GMPPNP Deposited 2005-03-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 69–451（383 aa）	Not recorded	MG MAGNESIUM ION × 4 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；293 K；PEG 2000-MME, magnesium sulphate, Tris buffer, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.00 Å R-free 0.285
1Z2C Crystal structure of mDIA1 GBD-FH3 in complex with RhoC-GMPPNP Deposited 2005-03-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 69–451（383 aa）	Not recorded	MG MAGNESIUM ION × 2 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；293 K；PEG 2000-MME, magnesium sulphate, Tris buffer, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.00 Å R-free 0.285
2BAP Crystal structure of the N-terminal mDia1 Armadillo Repeat Region and Dimerisation Domain in complex with the mDia1 autoregulatory domain (DAD) Deposited 2005-10-14	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 135–451（317 aa） Fragment：mDia1 N-terminal regulatory domain Chain C 1145–1200（56 aa） Fragment：mDia1 autoregulatory domain, DAD	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；3.7 M NaFormiate pH 7.1, 100 mM HEPES pH 7.1, 4% (w/v) PEG5000-MME, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.30 Å R-free 0.364
2BAP Crystal structure of the N-terminal mDia1 Armadillo Repeat Region and Dimerisation Domain in complex with the mDia1 autoregulatory domain (DAD) Deposited 2005-10-14	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain B 135–451（317 aa） Fragment：mDia1 N-terminal regulatory domain Chain D 1145–1200（56 aa） Fragment：mDia1 autoregulatory domain, DAD	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；293 K；3.7 M NaFormiate pH 7.1, 100 mM HEPES pH 7.1, 4% (w/v) PEG5000-MME, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.30 Å R-free 0.364
2BNX Crystal structure of the dimeric regulatory domain of mouse diaphaneous-related formin (DRF), mDia1 Deposited 2005-04-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 131–516（386 aa） Fragment：AMINO-TERMINAL DOMAIN, RESIDUES 131-516 Chain B 131–516（386 aa） Fragment：AMINO-TERMINAL DOMAIN, RESIDUES 131-516	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.25；HANGING DROP VAPOR DIFFUSION; PROTEIN: 11 MG/ML IN 100 MM HEPES, PH 7.25; RESERVOIR: 100 MM HEPES, PH 7.25, 9% PEG3350	Resolution 2.40 Å R-free 0.236
2V8F Mouse Profilin IIa in complex with a double repeat from the FH1 domain of mDia1 Deposited 2007-08-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 635–655（21 aa） Fragment：FH1 DOMAIN, RESIDUES 635-655	Not recorded	SO4 SULFATE ION × 5 NA SODIUM ION × 1 GOL GLYCEROL × 1 IPA ISOPROPYL ALCOHOL × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.10 Å R-free 0.173
3EG5 Crystal structure of MDIA1-TSH GBD-FH3 in complex with CDC42-GMPPNP Deposited 2008-09-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 69–451（383 aa） Fragment：MDIAN-TSH, UNP residues 69-451 Chain D 69–451（383 aa） Fragment：MDIAN-TSH, UNP residues 69-451	Mutation：N164T, N165S, N166H Mutation：N164T, N165S, N166H	GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；293 K；Bis-Tris-Propane (PH 8.8 adjusted with citric acid), 26% (w/v) PEG 3350, 250mM Na-Tartrate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.70 Å R-free 0.243
3O4X Crystal structure of complex between amino and carboxy terminal fragments of mDia1 Deposited 2010-07-27	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 131–458（328 aa） Fragment：mDia1 N-terminal regulatory domain (unp residues 131-458) Chain D 131–458（328 aa） Fragment：mDia1 N-terminal regulatory domain (unp residues 131-458) Chain E 736–1200（465 aa） Fragment：mDia1 C-terminal FH2-DAD domain (unp residues 736-1200) Chain H 736–1200（465 aa） Fragment：mDia1 C-terminal FH2-DAD domain (unp residues 736-1200)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；313 K；Peg 4000, sodium malonate, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 313K	Resolution 3.20 Å R-free 0.298
3O4X Crystal structure of complex between amino and carboxy terminal fragments of mDia1 Deposited 2010-07-27	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain B 131–458（328 aa） Fragment：mDia1 N-terminal regulatory domain (unp residues 131-458) Chain C 131–458（328 aa） Fragment：mDia1 N-terminal regulatory domain (unp residues 131-458) Chain F 736–1200（465 aa） Fragment：mDia1 C-terminal FH2-DAD domain (unp residues 736-1200) Chain G 736–1200（465 aa） Fragment：mDia1 C-terminal FH2-DAD domain (unp residues 736-1200)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；313 K；Peg 4000, sodium malonate, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 313K	Resolution 3.20 Å R-free 0.298
3OBV Autoinhibited Formin mDia1 Structure Deposited 2010-08-09	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: dimeric	Chain A 131–457（327 aa） Fragment：N-terminal fragment, UNP residues 131-457 Chain B 131–457（327 aa） Fragment：N-terminal fragment, UNP residues 131-457 Chain E 753–1209（457 aa） Fragment：C-terminal fragment, UNP residues 753-1209 Chain F 753–1209（457 aa） Fragment：C-terminal fragment, UNP residues 753-1209	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.75；293 K；10% PEG 1500, 25% sucrose, 0.1 M MES pH 6.75, 0.15 M NaCl, 1 mM DTT, vapor diffusion, hanging drop, temperature 293K	Resolution 2.75 Å R-free 0.261
3OBV Autoinhibited Formin mDia1 Structure Deposited 2010-08-09	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 4 PDB declaration: dimeric	Chain C 131–457（327 aa） Fragment：N-terminal fragment, UNP residues 131-457 Chain D 131–457（327 aa） Fragment：N-terminal fragment, UNP residues 131-457 Chain G 753–1209（457 aa） Fragment：C-terminal fragment, UNP residues 753-1209 Chain H 753–1209（457 aa） Fragment：C-terminal fragment, UNP residues 753-1209	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.75；293 K；10% PEG 1500, 25% sucrose, 0.1 M MES pH 6.75, 0.15 M NaCl, 1 mM DTT, vapor diffusion, hanging drop, temperature 293K	Resolution 2.75 Å R-free 0.261
4UWX Structure of liprin-alpha3 in complex with mDia1 Diaphanous- inhibitory domain Deposited 2014-08-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 135–369（235 aa） Fragment：DIAPHANOUS-INHIBITORY DOMAIN, RESIDUES 135-369	Not recorded	NI NICKEL (II) ION × 1 144 TRIS-HYDROXYMETHYL-METHYL-AMMONIUM × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；0.2 M NACL, 0.1 M TRIS/HCL PH 8.0, 20% PEG6000	Resolution 1.65 Å R-free 0.210
4UWX Structure of liprin-alpha3 in complex with mDia1 Diaphanous- inhibitory domain Deposited 2014-08-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 135–369（235 aa） Fragment：DIAPHANOUS-INHIBITORY DOMAIN, RESIDUES 135-369	Not recorded	NI NICKEL (II) ION × 1 144 TRIS-HYDROXYMETHYL-METHYL-AMMONIUM × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；0.2 M NACL, 0.1 M TRIS/HCL PH 8.0, 20% PEG6000	Resolution 1.65 Å R-free 0.210
8RU2 Structure of the F-actin barbed end bound by formin mDia1 Deposited 2024-01-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 552–584（33 aa） Chain E 721–1255（535 aa） Chain F 552–584（33 aa） Chain F 721–1255（535 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.1 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；3 seconds, force 0.	Resolution 3.49 Å
9B27 Dia1 at the Barbed End of F-Actin Deposited 2024-03-14	Different construct 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 G 745–1166（422 aa） Chain H 745–1166（422 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.51 Å
9B3D mDia1 in the middle of F-actin Deposited 2024-03-19	Different construct 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 G 745–1143（399 aa） Chain H 745–1143（399 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8；20mM HEPES, 50mM NaCL, 1mM EDTA, 1mM DTT, 0.05% Thesit cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.41 Å

12 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	DIAP1_MOUSE
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–233； UniProt 135–367 Author chain B； PDBConstruct 1–20； UniProt 1177–1196

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	2f31
Deposition date deposition_date	2005-11-18
Structure title title	Crystal structure of the autoinhibitory switch in Formin mDia1; the DID/DAD complex
Keywords keywords	formin, mDia1, protein-protein complex, armadillo repeats, 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	19.77 Å
Radius of gyration Rg (electron density) rg_electron	18.53 Å
Forward intensity I(0) i0	14511300.00
Molecular weight molecular_weight	28118.0 kDa
Excluded volume excluded_volume	35080 Å³
Envelope volume envelope_volume	41276 Å³
Hydration-shell volume shell_volume	18735 Å³
Envelope diameter envelope_diameter	65.7 Å
Shell Rg shell_rg	24.63 Å
Envelope Rg envelope_rg	18.85 Å
Shape Rg shape_rg	18.57 Å
Total Rg total_rg	19.31 Å
Total atoms total_atoms	1962
Residues n_residues	248
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	65.7 Å
Rg (real space) rg_real	19.70 Å
Rg uncertainty (real space) rg_real_error	0.34 Å
I(0) (real space) i0_real	1.4510e+07
I(0) uncertainty (real space) i0_real_error	1.7280e+05
Rg (reciprocal space) rg_reciprocal	19.71 Å
I(0) (reciprocal space) i0_reciprocal	14510000.0000
Solution quality estimate total_estimate	0.6986
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	23.1 Å
Skewness Skewness skewness	0.289
Kurtosis Kurtosis kurtosis	-0.323
Angular range angular_range	— – 0.4000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3545000.0000
Real-space data points n_real_points	72
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.825; Stabil: 1.000; Sysdev: 0.210; Positv: 1.000; Valcen: 0.994; Smooth: 0.979

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Diaphanous protein homolog 1
Molecular weight formula_weight	26592.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2087

SAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDL

来源 Source

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)

Entity 2 Entity 2 polymer

Description description	Diaphanous protein homolog 1
Molecular weight formula_weight	2111.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

DETGVMDSLLEALQSGAAFR

来源 Source

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)

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	125

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	2f31A00
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily	10 — Leucine-rich Repeat Variant

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8. Citations (1)

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Unit-cell length a length_a	102.160 Å
Unit-cell length b length_b	65.790 Å
Unit-cell length c length_c	46.860 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	104.08 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	7.970 Å
R factor r_factor	0.2328
R_work r_work	0.2287
R_free r_free	0.3117

fit	/app/data/saxs_computation/f3/2f31/2f31.fit
pddf	/app/data/pr_computation/f3/2f31/2f31.pr.out
profile	/app/data/saxs_computation/f3/2f31/2f31.dat

Crystal structure of the autoinhibitory switch in Formin mDia1; the DID/DAD complex

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

Diaphanous protein homolog 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

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)