7bhe

DARPin_D5/Her3 domain 4 complex, monoclinic crystals

Method: X-RAY DIFFRACTION Dmax: 103.6 Å Quality: GOOD

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

Receptor tyrosine-protein kinase erbB-3

Homo sapiens

UniProt P21860

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 B; UniProt 500–643 Not recorded DARPin_D5 × 1 GOL GLYCEROL × 2 ACT ACETATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 4.83;293 K;0.1 M Na citrate, 12% PEG4000, 0.2 M Li sulfate Resolution 2.30 Å R-free 0.254
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 500–643 Not recorded DARPin_D5 × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 4.83;293 K;0.1 M Na citrate, 12% PEG4000, 0.2 M Li sulfate Resolution 2.30 Å R-free 0.254

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.

22 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ERBB3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 7–150; UniProt 500–643 Author chain D; PDBConstruct 7–150; UniProt 500–643

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 7bhe

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7bhe
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7bhe
Deposition date deposition_date2021-01-11
Structure title titleDARPin_D5/Her3 domain 4 complex, monoclinic crystals
Keywords keywordsdesigned ankyrin repeat protein, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.91
Radius of gyration Rg (electron density) rg_electron30.58
Forward intensity I(0) i057913400.00
Molecular weight molecular_weight55170.0 kDa
Excluded volume excluded_volume66821 ų
Envelope volume envelope_volume91611 ų
Hydration-shell volume shell_volume25449 ų
Envelope diameter envelope_diameter108.0
Shell Rg shell_rg37.16
Envelope Rg envelope_rg29.86
Shape Rg shape_rg30.58
Total Rg total_rg31.13
Total atoms total_atoms3848
Residues n_residues514
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 dmax103.6
Rg (real space) rg_real31.00
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real5.7910e+07
I(0) uncertainty (real space) i0_real_error1.0460e+06
Rg (reciprocal space) rg_reciprocal30.97
I(0) (reciprocal space) i0_reciprocal57910000.0000
Solution quality estimate total_estimate0.8788
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.4
Skewness Skewness skewness0.287
Kurtosis Kurtosis kurtosis-0.612
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3585000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.888; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.805; Smooth: 0.950

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)