3o4x

Crystal structure of complex between amino and carboxy terminal fragments of mDia1

Method: X-RAY DIFFRACTION D_max: 164.7 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	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 131–458 Chain D； UniProt 131–458 Chain E； UniProt 736–1200 Chain H； UniProt 736–1200	Fragment：mDia1 N-terminal regulatory domain (unp residues 131-458) Fragment：mDia1 C-terminal FH2-DAD domain (unp residues 736-1200)	No other associated polymer	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
2	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain B； UniProt 131–458 Chain C； UniProt 131–458 Chain F； UniProt 736–1200 Chain G； UniProt 736–1200	Fragment：mDia1 N-terminal regulatory domain (unp residues 131-458) Fragment：mDia1 C-terminal FH2-DAD domain (unp residues 736-1200)	No other associated polymer	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

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 3O4X	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 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 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 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 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
3OBV Autoinhibited Formin mDia1 Structure Deposited 2010-08-09	Different construct 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 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 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 3–330； UniProt 131–458 Author chain B； PDBConstruct 3–330； UniProt 131–458 Author chain C； PDBConstruct 3–330； UniProt 131–458 Author chain D； PDBConstruct 3–330； UniProt 131–458 Author chain E； PDBConstruct 3–467； UniProt 736–1200 Author chain F； PDBConstruct 3–467； UniProt 736–1200 Author chain G； PDBConstruct 3–467； UniProt 736–1200 Author chain H； PDBConstruct 3–467； UniProt 736–1200

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	3o4x
Deposition date deposition_date	2010-07-27
Structure title title	Crystal structure of complex between amino and carboxy terminal fragments of mDia1
Keywords keywords	autoinhibition, actin nucleator, actin binding, PROTEIN BINDING; PROTEIN BINDING
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	52.30 Å
Radius of gyration Rg (electron density) rg_electron	51.76 Å
Forward intensity I(0) i0	1728460000.00
Molecular weight molecular_weight	346570.0 kDa
Excluded volume excluded_volume	434200 Å³
Envelope volume envelope_volume	669920 Å³
Hydration-shell volume shell_volume	106450 Å³
Envelope diameter envelope_diameter	168.1 Å
Shell Rg shell_rg	56.79 Å
Envelope Rg envelope_rg	50.22 Å
Shape Rg shape_rg	51.71 Å
Total Rg total_rg	52.10 Å
Total atoms total_atoms	24287
Residues n_residues	2997
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	164.7 Å
Rg (real space) rg_real	52.06 Å
Rg uncertainty (real space) rg_real_error	0.97 Å
I(0) (real space) i0_real	1.7280e+09
I(0) uncertainty (real space) i0_real_error	3.1390e+07
Rg (reciprocal space) rg_reciprocal	52.48 Å
I(0) (reciprocal space) i0_reciprocal	1729000000.0000
Solution quality estimate total_estimate	0.8112
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	71.4 Å
Skewness Skewness skewness	0.110
Kurtosis Kurtosis kurtosis	-0.379
Angular range angular_range	— – 0.1500 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	236700000.0000
Real-space data points n_real_points	31
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.862; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; Smooth: 0.000

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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	37993.6 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	24335

GSESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDLKGRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECVSQIVLHKNGTDPDFKCRHLQIDIERLVDQ

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	53872.7 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

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

GSFGFGVPAAPVLPFGLTPKKVYKPEVQLRRPNWSKFVAEDLSQDCFWTKVKEDRFENNELFAKLTLAFSAQTKTSKAKKDQEGGEEKKSVQKKKVKELKVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMGTVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLRDTKSADQKMTLLHFLAELCENDHPEVLKFPDELAHVEKASRVSAENLQKSLDQMKKQIADVERDVQNFPAATDEKDKFVEKMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRRETEEKMRRAKLAKEKAEKERLEKQQKREQLIDMNAEGDETGVMDSLLEALQSGAAFRRKRG

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 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	48

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7. Fold Classification (SCOP + CATH) 20 domains

CATH v4.4 (20 domains)

Domain ID domain_id	3o4xA01
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	3o4xA02
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	3o4xB01
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	3o4xB02
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	3o4xC01
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	3o4xC02
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	3o4xD01
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	3o4xD02
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	3o4xE01
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	30 — Lyase 2-enoyl-coa Hydratase; Chain A, domain 2
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3o4xE02
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	3o4xE03
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	3o4xF01
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	30 — Lyase 2-enoyl-coa Hydratase; Chain A, domain 2
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3o4xF02
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	3o4xF03
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	3o4xG01
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	30 — Lyase 2-enoyl-coa Hydratase; Chain A, domain 2
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3o4xG02
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	3o4xG03
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	3o4xH01
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	30 — Lyase 2-enoyl-coa Hydratase; Chain A, domain 2
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3o4xH02
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	3o4xH03
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	95.762 Å
Unit-cell length b length_b	206.832 Å
Unit-cell length c length_c	131.065 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	105.94 °
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	3.200 Å
Low-resolution limit resolution_low	20.120 Å
R factor r_factor	0.2359
R_work r_work	0.2326
R_free r_free	0.2983

fit	/app/data/saxs_computation/o4/3o4x/3o4x.fit
pddf	/app/data/pr_computation/o4/3o4x/3o4x.pr.out
profile	/app/data/saxs_computation/o4/3o4x/3o4x.dat

Crystal structure of complex between amino and carboxy terminal fragments of mDia1

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 water

7. Fold Classification (SCOP + CATH) 20 domains

CATH v4.4 (20 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)