4p3w

Crystal structure of the human filamin A Ig-like domains 20-21 in complex with migfilin peptide

Method: X-RAY DIFFRACTION Dmax: 136.5 Å Quality: GOOD

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

Filamin-A

Homo sapiens

UniProt P21333

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2152–2329 Fragment:Filamin repeats 20 and 21, residues 2152-2329 Filamin-binding LIM protein 1 × 1 (Q8WUP2) SO4 SULFATE ION × 1 PR PRASEODYMIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;0.1 M MES pH 6, 1.9 M (NH4)2SO4, 0.1 M (CH3CO2)3Pr Resolution 2.00 Å R-free 0.226
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2152–2329 Fragment:Filamin repeats 20 and 21, residues 2152-2329 Filamin-binding LIM protein 1 × 1 (Q8WUP2) SO4 SULFATE ION × 1 PR PRASEODYMIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;0.1 M MES pH 6, 1.9 M (NH4)2SO4, 0.1 M (CH3CO2)3Pr Resolution 2.00 Å R-free 0.226
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 2152–2329 Fragment:Filamin repeats 20 and 21, residues 2152-2329 Filamin-binding LIM protein 1 × 1 (Q8WUP2) SO4 SULFATE ION × 1 PR PRASEODYMIUM ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;0.1 M MES pH 6, 1.9 M (NH4)2SO4, 0.1 M (CH3CO2)3Pr Resolution 2.00 Å R-free 0.226
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 2152–2329 Fragment:Filamin repeats 20 and 21, residues 2152-2329 Filamin-binding LIM protein 1 × 1 (Q8WUP2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;0.1 M MES pH 6, 1.9 M (NH4)2SO4, 0.1 M (CH3CO2)3Pr Resolution 2.00 Å R-free 0.226
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 2152–2329 Fragment:Filamin repeats 20 and 21, residues 2152-2329 Filamin-binding LIM protein 1 × 1 (Q8WUP2) PR PRASEODYMIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;0.1 M MES pH 6, 1.9 M (NH4)2SO4, 0.1 M (CH3CO2)3Pr Resolution 2.00 Å R-free 0.226
6 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 2152–2329 Fragment:Filamin repeats 20 and 21, residues 2152-2329 Filamin-binding LIM protein 1 × 1 (Q8WUP2) SO4 SULFATE ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;0.1 M MES pH 6, 1.9 M (NH4)2SO4, 0.1 M (CH3CO2)3Pr Resolution 2.00 Å R-free 0.226

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.

25 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLNA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–182; UniProt 2152–2329 Author chain B; PDBConstruct 5–182; UniProt 2152–2329 Author chain C; PDBConstruct 5–182; UniProt 2152–2329 Author chain D; PDBConstruct 5–182; UniProt 2152–2329 Author chain E; PDBConstruct 5–182; UniProt 2152–2329 Author chain F; PDBConstruct 5–182; UniProt 2152–2329

Filamin-binding LIM protein 1

OrganismNot specified

UniProt Q8WUP2

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 5–28 Fragment:residues 5-28 Filamin-A × 1 (P21333) SO4 SULFATE ION × 1 PR PRASEODYMIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;0.1 M MES pH 6, 1.9 M (NH4)2SO4, 0.1 M (CH3CO2)3Pr Resolution 2.00 Å R-free 0.226
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 5–28 Fragment:residues 5-28 Filamin-A × 1 (P21333) SO4 SULFATE ION × 1 PR PRASEODYMIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;0.1 M MES pH 6, 1.9 M (NH4)2SO4, 0.1 M (CH3CO2)3Pr Resolution 2.00 Å R-free 0.226
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain K; UniProt 5–28 Fragment:residues 5-28 Filamin-A × 1 (P21333) SO4 SULFATE ION × 1 PR PRASEODYMIUM ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;0.1 M MES pH 6, 1.9 M (NH4)2SO4, 0.1 M (CH3CO2)3Pr Resolution 2.00 Å R-free 0.226
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain L; UniProt 5–28 Fragment:residues 5-28 Filamin-A × 1 (P21333) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;0.1 M MES pH 6, 1.9 M (NH4)2SO4, 0.1 M (CH3CO2)3Pr Resolution 2.00 Å R-free 0.226
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain J; UniProt 5–28 Fragment:residues 5-28 Filamin-A × 1 (P21333) PR PRASEODYMIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;0.1 M MES pH 6, 1.9 M (NH4)2SO4, 0.1 M (CH3CO2)3Pr Resolution 2.00 Å R-free 0.226
6 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 5–28 Fragment:residues 5-28 Filamin-A × 1 (P21333) SO4 SULFATE ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;0.1 M MES pH 6, 1.9 M (NH4)2SO4, 0.1 M (CH3CO2)3Pr Resolution 2.00 Å R-free 0.226

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FBLI1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–24; UniProt 5–28 Author chain H; PDBConstruct 1–24; UniProt 5–28 Author chain I; PDBConstruct 1–24; UniProt 5–28 Author chain J; PDBConstruct 1–24; UniProt 5–28 Author chain K; PDBConstruct 1–24; UniProt 5–28 Author chain L; PDBConstruct 1–24; UniProt 5–28

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 4p3w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4p3w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4p3w
Deposition date deposition_date2014-03-10
Structure title titleCrystal structure of the human filamin A Ig-like domains 20-21 in complex with migfilin peptide
Keywords keywordscytoskeleton, adhesion, immunoglobulin-like, actin binding protein, Cell Adhesion; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.51
Radius of gyration Rg (electron density) rg_electron40.71
Forward intensity I(0) i0207435000.00
Molecular weight molecular_weight113830.0 kDa
Excluded volume excluded_volume140910 ų
Envelope volume envelope_volume192180 ų
Hydration-shell volume shell_volume43046 ų
Envelope diameter envelope_diameter147.2
Shell Rg shell_rg41.56
Envelope Rg envelope_rg40.39
Shape Rg shape_rg40.69
Total Rg total_rg40.84
Total atoms total_atoms7983
Residues n_residues1090
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 dmax136.5
Rg (real space) rg_real40.90
Rg uncertainty (real space) rg_real_error1.39
I(0) (real space) i0_real2.0740e+08
I(0) uncertainty (real space) i0_real_error3.4030e+06
Rg (reciprocal space) rg_reciprocal40.51
I(0) (reciprocal space) i0_reciprocal207300000.0000
Solution quality estimate total_estimate0.7711
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.5
Skewness Skewness skewness0.572
Kurtosis Kurtosis kurtosis-0.365
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha96910000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.703; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.576; Smooth: 0.336

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id4p3wA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4p3wA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4p3wB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4p3wB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4p3wC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4p3wC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4p3wD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4p3wD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4p3wE01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4p3wE02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4p3wF01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4p3wF02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)