9dao

AlphaIIbbeta3 in fully-extended conformation in complex with R6H8 Fab

Method: ELECTRON MICROSCOPY Dmax: 146.0 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 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 32–1039 Not recorded Integrin beta-3 × 1 (P05106) R6H8 Fab heavy chain × 1 R6H8 Fab light chain × 1 CA CALCIUM ION × 5 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 1–1008; UniProt 32–1039

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 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 27–788 Not recorded Integrin alpha-IIb × 1 (P08514) R6H8 Fab heavy chain × 1 R6H8 Fab light chain × 1 CA CALCIUM ION × 5 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 1–762; UniProt 27–788

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 9dao

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9dao
Deposition date deposition_date2024-08-22
Structure title titleAlphaIIbbeta3 in fully-extended conformation in complex with R6H8 Fab
Keywords keywordsalphaIIbbeta3 integrin, platelet aggregation, clot retraction, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.01
Radius of gyration Rg (electron density) rg_electron41.98
Forward intensity I(0) i0298747000.00
Molecular weight molecular_weight138750.0 kDa
Excluded volume excluded_volume172690 ų
Envelope volume envelope_volume235960 ų
Hydration-shell volume shell_volume50380 ų
Envelope diameter envelope_diameter156.8
Shell Rg shell_rg42.87
Envelope Rg envelope_rg42.63
Shape Rg shape_rg41.94
Total Rg total_rg42.16
Total atoms total_atoms9763
Residues n_residues1264
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 dmax146.0
Rg (real space) rg_real42.28
Rg uncertainty (real space) rg_real_error1.39
I(0) (real space) i0_real2.9870e+08
I(0) uncertainty (real space) i0_real_error5.3750e+06
Rg (reciprocal space) rg_reciprocal42.01
I(0) (reciprocal space) i0_reciprocal298700000.0000
Solution quality estimate total_estimate0.8376
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.4
Skewness Skewness skewness0.480
Kurtosis Kurtosis kurtosis-0.363
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41710000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.759; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.893; Smooth: 0.716

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)