3obv

Autoinhibited Formin mDia1 Structure

Method: X-RAY DIFFRACTION D_max: 249.0 Å Quality: GOOD

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

Protein diaphanous 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	Other combination Homooligomer Protein × 4 其他Polymer 4 PDB declaration: dimeric（2） Count mismatch; review required	Chain A； UniProt 131–457 Chain B； UniProt 131–457 Chain E； UniProt 753–1209 Chain F； UniProt 753–1209	Fragment：N-terminal fragment, UNP residues 131-457 Fragment：C-terminal fragment, UNP residues 753-1209	beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose × 4	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
2	Other combination Homooligomer Protein × 4 其他Polymer 4 PDB declaration: dimeric（2） Count mismatch; review required	Chain C； UniProt 131–457 Chain D； UniProt 131–457 Chain G； UniProt 753–1209 Chain H； UniProt 753–1209	Fragment：N-terminal fragment, UNP residues 131-457 Fragment：C-terminal fragment, UNP residues 753-1209	beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose × 4	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

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 3OBV	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 oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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
2F31 Crystal structure of the autoinhibitory switch in Formin mDia1; the DID/DAD complex Deposited 2005-11-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 135–367（233 aa） Chain B 1177–1196（20 aa）	Not recorded	No recorded non-water small molecule	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
2F31 Crystal structure of the autoinhibitory switch in Formin mDia1; the DID/DAD complex Deposited 2005-11-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 135–367（233 aa） Chain B 1177–1196（20 aa）	Not recorded	No recorded non-water small molecule	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
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 oligomeric state 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 oligomeric state 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
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 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 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 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 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 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 1–327； UniProt 131–457 Author chain B； PDBConstruct 1–327； UniProt 131–457 Author chain C； PDBConstruct 1–327； UniProt 131–457 Author chain D； PDBConstruct 1–327； UniProt 131–457 Author chain E； PDBConstruct 1–457； UniProt 753–1209 Author chain F； PDBConstruct 1–457； UniProt 753–1209 Author chain G； PDBConstruct 1–457； UniProt 753–1209 Author chain H； PDBConstruct 1–457； UniProt 753–1209

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3obv
Deposition date deposition_date	2010-08-09
Structure title title	Autoinhibited Formin mDia1 Structure
Keywords keywords	AUTOINHIBITION, ACTIN, NUCLEATION, CYTOSKELETON, 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	68.25 Å
Radius of gyration Rg (electron density) rg_electron	68.83 Å
Forward intensity I(0) i0	1715420000.00
Molecular weight molecular_weight	345860.0 kDa
Excluded volume excluded_volume	432500 Å³
Envelope volume envelope_volume	803950 Å³
Hydration-shell volume shell_volume	102010 Å³
Envelope diameter envelope_diameter	246.5 Å
Shell Rg shell_rg	62.35 Å
Envelope Rg envelope_rg	67.41 Å
Shape Rg shape_rg	68.86 Å
Total Rg total_rg	68.58 Å
Total atoms total_atoms	24400
Residues n_residues	2967
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	249.0 Å
Rg (real space) rg_real	68.46 Å
Rg uncertainty (real space) rg_real_error	2.74 Å
I(0) (real space) i0_real	1.7160e+09
I(0) uncertainty (real space) i0_real_error	3.7540e+07
Rg (reciprocal space) rg_reciprocal	67.64 Å
I(0) (reciprocal space) i0_reciprocal	1713000000.0000
Solution quality estimate total_estimate	0.8018
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	75.8 Å
Skewness Skewness skewness	0.474
Kurtosis Kurtosis kurtosis	-0.070
Angular range angular_range	— – 0.1150 Å⁻¹
Current regularization parameter α current_alpha	0.0026
Highest regularization parameter α highest_alpha	77650000.0000
Real-space data points n_real_points	24
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.534; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.817

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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	Protein diaphanous homolog 1
Molecular weight formula_weight	37721.3 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	24400

ESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDLKGRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECVSQIVLHKNGTDPDFKCRHLQIDIERLVD

来源 Source

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

Entity 2 Entity 2 polymer

Description description	Protein diaphanous homolog 1
Molecular weight formula_weight	53069.8 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,G,H

KKVYKPEVQLRRPNWSKFVAEDLSQDCFWTKVKEDRFENNELFAKLTLAFSAQTKTSKAKKDQEGGEEKKSVQKKKVKELKVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMGTVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLRDTKSADQKMTLLHFLAELCENDHPEVLKFPDELAHVEKASRVSAENLQKSLDQMKKQIADVERDVQNFPAATDEKDKFVEKMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRRETEEKMRRAKLAKEKAEKERLEKQQKREQLIDMNAEGDETGVMDSLLEALQSGAAFRRKRGPRQVNRKAG

来源 Source

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

Entity 3 Entity 3 branched

Description description	beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose
Molecular weight formula_weight	342.3 kDa
Source method src_method	man
Copy count entity_count	8

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7. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3obva_
Class class	a — All alpha proteins
Fold Fold fold	a.118 — alpha-alpha superhelix
Superfamily Superfamily superfamily	a.118.1 — ARM repeat
Family Family family	a.118.1.23 — Diap1 N-terninal region-like

Domain ID domain_id	d3obvb_
Class class	a — All alpha proteins
Fold Fold fold	a.118 — alpha-alpha superhelix
Superfamily Superfamily superfamily	a.118.1 — ARM repeat
Family Family family	a.118.1.23 — Diap1 N-terninal region-like

Domain ID domain_id	d3obvc_
Class class	a — All alpha proteins
Fold Fold fold	a.118 — alpha-alpha superhelix
Superfamily Superfamily superfamily	a.118.1 — ARM repeat
Family Family family	a.118.1.23 — Diap1 N-terninal region-like

Domain ID domain_id	d3obvd_
Class class	a — All alpha proteins
Fold Fold fold	a.118 — alpha-alpha superhelix
Superfamily Superfamily superfamily	a.118.1 — ARM repeat
Family Family family	a.118.1.23 — Diap1 N-terninal region-like

CATH v4.4 (16 domains)

Domain ID domain_id	3obvA01
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

Domain ID domain_id	3obvA02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	150 — Formin, FH3 diaphanous domain

Domain ID domain_id	3obvB01
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

Domain ID domain_id	3obvB02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	150 — Formin, FH3 diaphanous domain

Domain ID domain_id	3obvC01
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

Domain ID domain_id	3obvC02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	150 — Formin, FH3 diaphanous domain

Domain ID domain_id	3obvD01
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

Domain ID domain_id	3obvD02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	150 — Formin, FH3 diaphanous domain

Domain ID domain_id	3obvE02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	630 —

Domain ID domain_id	3obvE03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	2220 — Formin, FH2 domain

Domain ID domain_id	3obvF02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	630 —

Domain ID domain_id	3obvF03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	2220 — Formin, FH2 domain

Domain ID domain_id	3obvG02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	630 —

Domain ID domain_id	3obvG03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	2220 — Formin, FH2 domain

Domain ID domain_id	3obvH02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	630 —

Domain ID domain_id	3obvH03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	2220 — Formin, FH2 domain

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8. Citations (1)

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Unit-cell length a length_a	93.926 Å
Unit-cell length b length_b	208.519 Å
Unit-cell length c length_c	131.516 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	102.74 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.750 Å
Low-resolution limit resolution_low	29.950 Å
R factor r_factor	0.2000
R_work r_work	0.1990
R_free r_free	0.2610

fit	/app/data/saxs_computation/ob/3obv/3obv.fit
pddf	/app/data/pr_computation/ob/3obv/3obv.pr.out
profile	/app/data/saxs_computation/ob/3obv/3obv.dat

Autoinhibited Formin mDia1 Structure

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

Protein diaphanous 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 branched

7. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (4 domains)

CATH v4.4 (16 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)