SAXSdb — 1v05

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

FILAMIN C

HOMO SAPIENS

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 2633–2725	Fragment：ROD DOMAIN, RESIDUES 2633-2725	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；1.6M NA CITRATE, 0.1M HEPES, PH7.5, pH 7.50	Resolution 1.43 Å R-free 0.205

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 1V05	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2D7M Solution structure of the 14th Filamin domain from human Filamin C Deposited 2005-11-24	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1536–1637（102 aa） Fragment：Filamin domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；296 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 1.22mM Filamin domain U-15N,13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2D7N Solution structure of the 16th Filamin domain from human Filamin C Deposited 2005-11-24	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1782–1861（80 aa） Fragment：Filamin domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；296 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 1.19mM Filamin domain U-15N,13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2D7O Solution structure of the 17th Filamin domain from human Filamin C Deposited 2005-11-24	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1856–1953（98 aa） Fragment：Filamin domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 1.16mM Filamin domain U-15N,13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2D7P Solution structure of the 22th Filamin domain from human Filamin C Deposited 2005-11-24	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2402–2500（99 aa） Fragment：Filamin domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；296 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 1.24mM Filamin domain U-15N,13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2D7Q Solution structure of the 23th Filamin domain from human Filamin C Deposited 2005-11-24	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2500–2599（100 aa） Fragment：Filamin domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；296 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 1.13mM Filamin domain U-15N,13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2NQC Crystal structure of ig-like domain 23 from human filamin C Deposited 2006-10-31	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2495–2598（104 aa） Fragment：Ig-like domain 23	Not recorded	NI NICKEL (II) ION × 1 IMD IMIDAZOLE × 2 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；17.5% PEG 10000, 0.2M imidazole malate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.05 Å R-free 0.237
3V8O Human Filamin C Ig - like Domains 4 and 5 Deposited 2011-12-23	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 569–761（193 aa） Fragment：Domains 4 and 5 (UNP residues 569-761)	Not recorded	K POTASSIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；1.6M Sodium Potassium Phosphate, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.80 Å R-free 0.255
3V8O Human Filamin C Ig - like Domains 4 and 5 Deposited 2011-12-23	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 569–761（193 aa） Fragment：Domains 4 and 5 (UNP residues 569-761)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；1.6M Sodium Potassium Phosphate, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.80 Å R-free 0.255
4MGX Crystal structure of human filamin C domains 4-5 and GPIB alpha cytoplasmic domain complex Deposited 2013-08-29	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 572–756（185 aa） Fragment：domains 4 and 5 (UNP residues 572-756)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；297 K；0.1 M HEPES, pH 7.5, 20% w/v PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 297K	Resolution 3.16 Å R-free 0.277
7OUU Crystal structure of human filamin C domains 14-15 Deposited 2021-06-13	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1534–1736（203 aa） Chain B 1534–1736（203 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；295.15 K；0.1 M HEPES 7.0, 30 % v/v Jeffamine ED-2003	Resolution 1.47 Å R-free 0.228
7OUV Crystal structure of human filamin C domains 14-15 cardiovascular disease causing mutation S1624L Deposited 2021-06-13	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1534–1736（203 aa） Chain B 1534–1736（203 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；295.15 K；0.1 M SPG pH 5.0, 25% w/v PEG 1500	Resolution 1.80 Å R-free 0.240
7P0E Crystal structure of human filamin C domains 14-15 cardiovascular disease causing mutation G1676R Deposited 2021-06-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1534–1736（203 aa） Chain B 1534–1736（203 aa）	Not recorded	GOL GLYCEROL × 4 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6；295.15 K；0.1 M BIS-TRIS pH 6.0, 26.3 % w/v PEG 3350, 5% w/v Glycerol	Resolution 1.60 Å R-free 0.221
8PA0 cvHsp (HspB7) C131S alpha-crystallin domain - filamin C (FLNC) domain 24 complex Deposited 2023-06-06	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2630–2725（96 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 mM HEPES and 20% w/v PEG 8000, pH 7.0	Resolution 2.85 Å R-free 0.291

12 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FLNC_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–96； UniProt 2633–2725

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	1v05
Deposition date deposition_date	2004-03-22
Structure title title	Dimerization of human Filamin C: crystal structure of the domain 24
Keywords keywords	ACTIN-BINDING PROTEIN, IMMUNOGLOBULIN; ACTIN-BINDING 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	14.61 Å
Radius of gyration Rg (electron density) rg_electron	13.49 Å
Forward intensity I(0) i0	2268620.00
Molecular weight molecular_weight	10373.0 kDa
Excluded volume excluded_volume	13003 Å³
Envelope volume envelope_volume	14757 Å³
Hydration-shell volume shell_volume	9776 Å³
Envelope diameter envelope_diameter	50.5 Å
Shell Rg shell_rg	18.46 Å
Envelope Rg envelope_rg	13.92 Å
Shape Rg shape_rg	13.43 Å
Total Rg total_rg	14.81 Å
Total atoms total_atoms	725
Residues n_residues	96
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	52.6 Å
Rg (real space) rg_real	14.62 Å
Rg uncertainty (real space) rg_real_error	0.42 Å
I(0) (real space) i0_real	2.2690e+06
I(0) uncertainty (real space) i0_real_error	2.8860e+04
Rg (reciprocal space) rg_reciprocal	14.62 Å
I(0) (reciprocal space) i0_reciprocal	2269000.0000
Solution quality estimate total_estimate	0.6708
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	16.0 Å
Skewness Skewness skewness	0.364
Kurtosis Kurtosis kurtosis	-0.240
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	633700.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.695; Stabil: 1.000; Sysdev: 0.256; Positv: 1.000; Valcen: 0.863; Smooth: 1.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1v05a1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.18 — E set domains
Family Family family	b.1.18.10 — Filamin repeat (rod domain)

Domain ID domain_id	d1v05a2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id	1v05A00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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8. Citations (1)

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Unit-cell length a length_a	48.099 Å
Unit-cell length b length_b	48.099 Å
Unit-cell length c length_c	117.485 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	12

Space group space_group	P 61 2 2
Space-group number int_tables_number	178
Crystal system crystal_system	—

Resolution resolution	1.430 Å
Low-resolution limit resolution_low	17.730 Å
R factor r_factor	0.1877
R_work r_work	0.1858
R_free r_free	0.2050

Description description	FILAMIN C
Molecular weight formula_weight	10383.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	804

Dimerization of human Filamin C: crystal structure of the domain 24

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

FILAMIN C

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	ESCHERICHIA COLI

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	73

fit	/app/data/saxs_computation/v0/1v05/1v05.fit
pddf	/app/data/pr_computation/v0/1v05/1v05.pr.out
profile	/app/data/saxs_computation/v0/1v05/1v05.dat