9qbh

HER2/ErbB2 extracellular domain (ECD) from a near full-length construct solubilized in amphipols.

Method: ELECTRON MICROSCOPY Dmax: 86.0 Å Quality: EXCELLENT

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

Receptor tyrosine-protein kinase erbB-2,Green fluorescent protein

Aequorea victoria

UniProt P04626

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 23–1029 Mutation:Del1-22,Del1030-1255,C789S,C805S,C965S. No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.77 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.

57 other PDB entries and 80 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ERBB2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 57–1063; UniProt 23–1029

Receptor tyrosine-protein kinase erbB-2,Green fluorescent protein

Aequorea victoria

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–238 Mutation:Del1-22,Del1030-1255,C789S,C805S,C965S. No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.77 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1074–1311; UniProt 1–238

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 9qbh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9qbh
Deposition date deposition_date2025-03-02
最后修订 last_revision2025-08-13
Structure title titleHER2/ErbB2 extracellular domain (ECD) from a near full-length construct solubilized in amphipols.
Keywords keywordsReceptor, tyrosine kinase, transmembrane, HER2, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier26.90
Radius of gyration Rg (electron density) rg_electron25.79
Forward intensity I(0) i056944000.00
Molecular weight molecular_weight56044.0 kDa
Excluded volume excluded_volume68995 ų
Envelope volume envelope_volume84665 ų
Hydration-shell volume shell_volume27875 ų
Envelope diameter envelope_diameter89.5
Shell Rg shell_rg32.57
Envelope Rg envelope_rg25.96
Shape Rg shape_rg25.75
Total Rg total_rg26.61
Total atoms total_atoms7682
Residues n_residues508
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 dmax86.0
Rg (real space) rg_real26.85
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real5.6940e+07
I(0) uncertainty (real space) i0_real_error7.5680e+05
Rg (reciprocal space) rg_reciprocal26.87
I(0) (reciprocal space) i0_reciprocal56940000.0000
Solution quality estimate total_estimate0.9053
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.1
Skewness Skewness skewness0.251
Kurtosis Kurtosis kurtosis-0.529
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4567000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.969

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)