9e8c

Integrin aIIbb3 dimer conformation from human platelet membrane crude preparation

Method: ELECTRON MICROSCOPY Dmax: 172.5 Å Quality: GOOD

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

Integrin alpha-IIb

OrganismNot specified

UniProt P08514

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 5 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1039 Chain C; UniProt 1–1039 Not recorded Integrin beta-3 × 2 (P05106) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-beta-D-mannopyranose × 1 CA CALCIUM ION × 12 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 Å

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.

76 other PDB entries and 116 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITA2B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1039; UniProt 1–1039 Author chain C; PDBConstruct 1–1039; UniProt 1–1039

Integrin beta-3

OrganismNot specified

UniProt P05106

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 5 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–788 Chain D; UniProt 1–788 Not recorded Integrin alpha-IIb × 2 (P08514) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-beta-D-mannopyranose × 1 CA CALCIUM ION × 12 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 Å

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.

124 other PDB entries and 176 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITB3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–788; UniProt 1–788 Author chain D; PDBConstruct 1–788; UniProt 1–788

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 9e8c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e8c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e8c
Deposition date deposition_date2024-11-05
最后修订 last_revision2025-10-15
Structure title titleIntegrin aIIbb3 dimer conformation from human platelet membrane crude preparation
Keywords keywordsplatelet membrane protein integrin aIIbb3, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.46
Radius of gyration Rg (electron density) rg_electron53.25
Forward intensity I(0) i0897813000.00
Molecular weight molecular_weight243660.0 kDa
Excluded volume excluded_volume302110 ų
Envelope volume envelope_volume440000 ų
Hydration-shell volume shell_volume70458 ų
Envelope diameter envelope_diameter175.6
Shell Rg shell_rg54.57
Envelope Rg envelope_rg51.73
Shape Rg shape_rg53.19
Total Rg total_rg53.47
Total atoms total_atoms17076
Residues n_residues2196
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 dmax172.5
Rg (real space) rg_real53.57
Rg uncertainty (real space) rg_real_error1.89
I(0) (real space) i0_real8.9780e+08
I(0) uncertainty (real space) i0_real_error1.8450e+07
Rg (reciprocal space) rg_reciprocal53.35
I(0) (reciprocal space) i0_reciprocal897500000.0000
Solution quality estimate total_estimate0.8524
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary65.4
Skewness Skewness skewness0.289
Kurtosis Kurtosis kurtosis-0.603
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha55610000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.263

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)