2jf1

CRYSTAL STRUCTURE OF THE FILAMIN A REPEAT 21 COMPLEXED WITH THE INTEGRIN BETA2 CYTOPLASMIC TAIL PEPTIDE

Method: X-RAY DIFFRACTION Dmax: 47.2 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 2236–2329 Fragment:IG 21, RESIDUES 2236-2329 INTEGRIN BETA-2 SUBUNIT × 3 (P05107) GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;1.6-1.58 M AMMONIUM SULPHATE, 0.1 M NA-ACETATE PH 4.6 Resolution 2.20 Å R-free 0.278

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 41 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 4–97; UniProt 2236–2329

INTEGRIN BETA-2 SUBUNIT

OrganismNot specified

UniProt P05107

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain T; UniProt 735–769 Fragment:RESIDUES 735-769 FILAMIN-A × 3 (P21333) GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;1.6-1.58 M AMMONIUM SULPHATE, 0.1 M NA-ACETATE PH 4.6 Resolution 2.20 Å R-free 0.278

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.

24 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITB2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain T; PDBConstruct 1–35; UniProt 735–769

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 2jf1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2jf1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2jf1
Deposition date deposition_date2007-01-25
Structure title titleCRYSTAL STRUCTURE OF THE FILAMIN A REPEAT 21 COMPLEXED WITH THE INTEGRIN BETA2 CYTOPLASMIC TAIL PEPTIDE
Keywords keywords;ACTIN-BINDING, CELL ADHESION, TRANSMEMBRANE, ACETYLATION, POLYMORPHISM, CYTOSKELETON, GLYCOPROTEIN, FILAMIN, COMPLEX, MEMBRANE, INTEGRIN, RECEPTOR, PYRROLIDONE CARBOXYLIC ACID, PHOSPHORYLATION, DISEASE MUTATION, IMMUNOGLOBULIN LIKE ;; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.23
Radius of gyration Rg (electron density) rg_electron12.94
Forward intensity I(0) i02235640.00
Molecular weight molecular_weight10244.0 kDa
Excluded volume excluded_volume12811 ų
Envelope volume envelope_volume14560 ų
Hydration-shell volume shell_volume9923 ų
Envelope diameter envelope_diameter45.8
Shell Rg shell_rg18.24
Envelope Rg envelope_rg13.31
Shape Rg shape_rg12.93
Total Rg total_rg14.22
Total atoms total_atoms723
Residues n_residues98
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 dmax47.2
Rg (real space) rg_real14.20
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real2.2360e+06
I(0) uncertainty (real space) i0_real_error2.3450e+04
Rg (reciprocal space) rg_reciprocal14.20
I(0) (reciprocal space) i0_reciprocal2236000.0000
Solution quality estimate total_estimate0.8722
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.7
Skewness Skewness skewness0.330
Kurtosis Kurtosis kurtosis-0.178
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha661600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.793; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.959

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2jf1a_
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)

CATH v4.4 (1 domains)

Domain ID domain_id2jf1A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)