2d7q

Solution structure of the 23th Filamin domain from human Filamin C

Method: SOLUTION NMR Dmax: 43.2 Å Quality: REASONABLE

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

Filamin-C

Homo sapiens

UniProt Q14315

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2500–2599 Fragment:Filamin domain No other associated polymer 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

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.

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 8–105; UniProt 2500–2599

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

SAXS profile for 2d7q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2d7q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2d7q
Deposition date deposition_date2005-11-24
Structure title titleSolution structure of the 23th Filamin domain from human Filamin C
Keywords keywords;beta-sandwich, immunoglobulin-like fold, filamin domain, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, STRUCTURAL PROTEIN ;; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier16.03
Radius of gyration Rg (electron density) rg_electron15.41
Forward intensity I(0) i0703978000.00
Molecular weight molecular_weight216640.0 kDa
Excluded volume excluded_volume268090 ų
Envelope volume envelope_volume41743 ų
Hydration-shell volume shell_volume16863 ų
Envelope diameter envelope_diameter86.9
Shell Rg shell_rg28.07
Envelope Rg envelope_rg23.62
Shape Rg shape_rg15.38
Total Rg total_rg15.83
Total atoms total_atoms30120
Residues n_residues2220
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax43.2
Rg (real space) rg_real14.89
Rg uncertainty (real space) rg_real_error0.08
I(0) (real space) i0_real6.6880e+08
I(0) uncertainty (real space) i0_real_error6.3950e+06
Rg (reciprocal space) rg_reciprocal16.29
I(0) (reciprocal space) i0_reciprocal704000000.0000
Solution quality estimate total_estimate0.6814
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.378
Kurtosis Kurtosis kurtosis-0.410
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha4.1870
Highest regularization parameter α highest_alpha303700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.011; Oscil: 0.970; Stabil: 0.987; Sysdev: 0.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2d7qa1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.10 — Filamin repeat (rod domain)
Domain ID domain_idd2d7qa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2d7qa3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2d7qA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)