6avu

Human alpha-V beta-3 Integrin (open conformation) in complex with the therapeutic antibody LM609

Method: ELECTRON MICROSCOPY Dmax: 217.0 Å Quality: GOOD

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

Integrin alpha-V

Homo sapiens

UniProt P06756

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 31–987 Fragment:UNP residues 31-987 Integrin beta-3 × 1 (P05106) Fab LM609 heavy chain × 1 Fab LM609 light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 Resolution 35.00 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.

55 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITAV_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–957; UniProt 31–987

Integrin beta-3

Homo sapiens

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 27–718 Fragment:UNP residues 27-718 Integrin alpha-V × 1 (P06756) Fab LM609 heavy chain × 1 Fab LM609 light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 Resolution 35.00 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 P05106-3
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–692; UniProt 27–718

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 6avu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6avu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6avu
Deposition date deposition_date2017-09-04
Structure title titleHuman alpha-V beta-3 Integrin (open conformation) in complex with the therapeutic antibody LM609
Keywords keywordsalpha-V beta-3 integrin, LM609, vitaxin, abegrin, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier59.65
Radius of gyration Rg (electron density) rg_electron61.51
Forward intensity I(0) i0349346000.00
Molecular weight molecular_weight124730.0 kDa
Excluded volume excluded_volume143230 ų
Envelope volume envelope_volume342980 ų
Hydration-shell volume shell_volume54443 ų
Envelope diameter envelope_diameter236.0
Shell Rg shell_rg49.28
Envelope Rg envelope_rg62.22
Shape Rg shape_rg61.54
Total Rg total_rg60.92
Total atoms total_atoms8913
Residues n_residues1809
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 dmax217.0
Rg (real space) rg_real60.88
Rg uncertainty (real space) rg_real_error3.08
I(0) (real space) i0_real3.4930e+08
I(0) uncertainty (real space) i0_real_error8.4620e+06
Rg (reciprocal space) rg_reciprocal58.61
I(0) (reciprocal space) i0_reciprocal348100000.0000
Solution quality estimate total_estimate0.7669
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary75.1
Skewness Skewness skewness0.725
Kurtosis Kurtosis kurtosis0.163
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0007
Highest regularization parameter α highest_alpha12480000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.518; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.739; Smooth: 0.672

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)