SAXSdb — 3eg5

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

Cell division control protein 42 homolog

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–178 Chain C； UniProt 1–178	Fragment：UNP residues 1-178	Protein diaphanous homolog 1 × 2 （O08808） 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

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 3EG5	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5C2J Complex structure of the GAP domain of MgcRacGAP and Cdc42 Deposited 2015-06-16	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 B 1–191（191 aa）	Not recorded	MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；PEG3350, Bis-Tris	Resolution 2.50 Å R-free 0.263

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CDC42_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–178； UniProt 1–178 Author chain C； PDBConstruct 1–178； UniProt 1–178

Protein diaphanous homolog 1

Mus musculus

UniProt O08808

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain B； UniProt 69–451 Chain D； UniProt 69–451	Fragment：MDIAN-TSH, UNP residues 69-451 Mutation：N164T, N165S, N166H	Cell division control protein 42 homolog × 2 （P60766） 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

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 3EG5	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 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 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 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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
3O4X Crystal structure of complex between amino and carboxy terminal fragments of mDia1 Deposited 2010-07-27	Different construct Different mutation/modification 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 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 oligomeric state Different ligand/ion 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 ligand/ion 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 ligand/ion 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 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 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	DIAP1_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–383； UniProt 69–451 Author chain D； PDBConstruct 1–383； UniProt 69–451

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	3eg5
Deposition date deposition_date	2008-09-10
Structure title title	Crystal structure of MDIA1-TSH GBD-FH3 in complex with CDC42-GMPPNP
Keywords keywords	;PROTEIN-PROTEIN COMPLEX, RHO PROTEINS, DIAPHANOUS, FORMINS, ARMADILLO REPEAT, G-PROTEIN, GTPASE, Alternative splicing, Cell membrane, GTP-binding, Lipoprotein, Membrane, Methylation, Nucleotide-binding, Prenylation, Actin-binding, Cell projection, Coiled coil, Cytoplasm, Cytoskeleton, Phosphoprotein, Ubl conjugation, SIGNALING PROTEIN ;; SIGNALING 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	39.87 Å
Radius of gyration Rg (electron density) rg_electron	39.76 Å
Forward intensity I(0) i0	211044000.00
Molecular weight molecular_weight	118560.0 kDa
Excluded volume excluded_volume	148710 Å³
Envelope volume envelope_volume	207680 Å³
Hydration-shell volume shell_volume	44022 Å³
Envelope diameter envelope_diameter	133.9 Å
Shell Rg shell_rg	45.17 Å
Envelope Rg envelope_rg	38.58 Å
Shape Rg shape_rg	39.76 Å
Total Rg total_rg	40.08 Å
Total atoms total_atoms	8294
Residues n_residues	1030
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	127.5 Å
Rg (real space) rg_real	39.89 Å
Rg uncertainty (real space) rg_real_error	1.06 Å
I(0) (real space) i0_real	2.1100e+08
I(0) uncertainty (real space) i0_real_error	3.9540e+06
Rg (reciprocal space) rg_reciprocal	39.89 Å
I(0) (reciprocal space) i0_reciprocal	211000000.0000
Solution quality estimate total_estimate	0.8821
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	35.0 Å
Skewness Skewness skewness	0.171
Kurtosis Kurtosis kurtosis	-0.830
Angular range angular_range	— – 0.2000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	23830000.0000
Real-space data points n_real_points	41
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.885; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.937; Smooth: 0.871

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Cell division control protein 42 homolog
Molecular weight formula_weight	19802.7 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	8341

MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQRGLKNVFDEAILAALE

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	44200.7 kDa
Mutation mutation	N164T, N165S, N166H
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

DPTAQSLQDISDEQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHTSKAGMNQKESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLTSHPVSWVQTFGAEGLASLLDILKRLHDEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDLKGRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECVSQIVLHKNGTDPDFKCRHLQID

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 non-polymer

Description description	PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
Molecular weight formula_weight	522.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	47

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3eg5a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.8 — G proteins

Domain ID domain_id	d3eg5b_
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	d3eg5c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.8 — G proteins

Domain ID domain_id	d3eg5d_
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 (8 domains)

Domain ID domain_id	3eg5A00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	3eg5B01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	20 — Histone, subunit A
Homologous superfamily homologous superfamily	40 — Formin, diaphanous GTPase-binding domain

Domain ID domain_id	3eg5B02
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	3eg5B03
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	3eg5C00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	3eg5D01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	20 — Histone, subunit A
Homologous superfamily homologous superfamily	40 — Formin, diaphanous GTPase-binding domain

Domain ID domain_id	3eg5D02
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	3eg5D03
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

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8. Citations (1)

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Unit-cell length a length_a	71.269 Å
Unit-cell length b length_b	71.269 Å
Unit-cell length c length_c	244.964 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 32
Space-group number int_tables_number	145
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	43.470 Å
R factor r_factor	0.2082
R_work r_work	0.2063
R_free r_free	0.2433

fit	/app/data/saxs_computation/eg/3eg5/3eg5.fit
pddf	/app/data/pr_computation/eg/3eg5/3eg5.pr.out
profile	/app/data/saxs_computation/eg/3eg5/3eg5.dat

Crystal structure of MDIA1-TSH GBD-FH3 in complex with CDC42-GMPPNP

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

Cell division control protein 42 homolog

State in the Current Structure

Other States of the Same Protein in the Database

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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)