2bp3

Crystal structure of Filamin A domain 17 and GPIb alpha cytoplasmic domain complex

Method: X-RAY DIFFRACTION Dmax: 64.3 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 1863–1956 Fragment:ROD DOMAIN, RESIDUES 1863-1956 PLATELET GLYCOPROTEIN IB ALPHA CHAIN × 1 (P07359) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.2;1.75M AMMONIUM PHOSPHATE, PH 8.2, AFTER MICROSEEDING: 1.25M AMMONIUM SULFATE PH 8.2 Resolution 2.32 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1863–1956 Fragment:ROD DOMAIN, RESIDUES 1863-1956 PLATELET GLYCOPROTEIN IB ALPHA CHAIN × 1 (P07359) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.2;1.75M AMMONIUM PHOSPHATE, PH 8.2, AFTER MICROSEEDING: 1.25M AMMONIUM SULFATE PH 8.2 Resolution 2.32 Å R-free 0.256

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 40 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 1863–1956 Author chain B; PDBConstruct 4–97; UniProt 1863–1956

PLATELET GLYCOPROTEIN IB ALPHA CHAIN

OrganismNot specified

UniProt P07359

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 T; UniProt 572–593 Fragment:CYTOPLASMIC DOMAIN, RESIDUES 572-593 FILAMIN A × 1 (P21333) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.2;1.75M AMMONIUM PHOSPHATE, PH 8.2, AFTER MICROSEEDING: 1.25M AMMONIUM SULFATE PH 8.2 Resolution 2.32 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain S; UniProt 572–593 Fragment:CYTOPLASMIC DOMAIN, RESIDUES 572-593 FILAMIN A × 1 (P21333) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.2;1.75M AMMONIUM PHOSPHATE, PH 8.2, AFTER MICROSEEDING: 1.25M AMMONIUM SULFATE PH 8.2 Resolution 2.32 Å R-free 0.256

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.

20 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GP1BA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain S; PDBConstruct 1–22; UniProt 572–593 Author chain T; PDBConstruct 1–22; UniProt 572–593

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 2bp3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2bp3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2bp3
Deposition date deposition_date2005-04-18
Structure title titleCrystal structure of Filamin A domain 17 and GPIb alpha cytoplasmic domain complex
Keywords keywordsSTRUCTURAL PROTEIN, CYTOSKELETON-COMPLEX, ACTIN BINDING PROTEIN, CYTOSKELETON, COMPLEX; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.95
Radius of gyration Rg (electron density) rg_electron19.11
Forward intensity I(0) i09230690.00
Molecular weight molecular_weight22200.0 kDa
Excluded volume excluded_volume27672 ų
Envelope volume envelope_volume33836 ų
Hydration-shell volume shell_volume15524 ų
Envelope diameter envelope_diameter65.2
Shell Rg shell_rg24.18
Envelope Rg envelope_rg19.21
Shape Rg shape_rg19.10
Total Rg total_rg19.95
Total atoms total_atoms1565
Residues n_residues213
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 dmax64.3
Rg (real space) rg_real19.94
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real9.2310e+06
I(0) uncertainty (real space) i0_real_error1.1300e+05
Rg (reciprocal space) rg_reciprocal19.95
I(0) (reciprocal space) i0_reciprocal9231000.0000
Solution quality estimate total_estimate0.8199
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.9
Skewness Skewness skewness0.288
Kurtosis Kurtosis kurtosis-0.495
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2289000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2bp3a1
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_idd2bp3b_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id2bp3A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2bp3B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)