6oge

Cryo-EM structure of Her2 extracellular domain-Trastuzumab Fab-Pertuzumab Fab complex

Method: ELECTRON MICROSCOPY Dmax: 144.4 Å Quality: GOOD

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

Receptor tyrosine-protein kinase erbB-2

Homo sapiens

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 Other combination Heteromer Protein × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 23–644 Not recorded Pertuzumab FAB LIGHT CHAIN × 1 (P01834) Pertuzumab FAB HEAVY CHAIN × 1 (P0DOX5) Trastuzumab FAB LIGHT CHAIN × 1 (P01834) Trastuzumab FAB HEAVY CHAIN × 1 (Q6GMX6) ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.36 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 1–622; UniProt 23–644

Pertuzumab FAB LIGHT CHAIN

Homo sapiens

UniProt P01834

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 × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–107 Chain D; UniProt 1–107 Not recorded Receptor tyrosine-protein kinase erbB-2 × 1 (P04626) Pertuzumab FAB HEAVY CHAIN × 1 (P0DOX5) Trastuzumab FAB HEAVY CHAIN × 1 (Q6GMX6) ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.36 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.

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

View Construct and Data Evidence
UniProt name IGKC_HUMAN
Isoform
PDB entities 2, 4
Chains and sequence ranges Author chain B; PDBConstruct 108–214; UniProt 1–107 Author chain D; PDBConstruct 108–214; UniProt 1–107

Pertuzumab FAB HEAVY CHAIN

Homo sapiens

UniProt P0DOX5

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 × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 109–222 Not recorded Receptor tyrosine-protein kinase erbB-2 × 1 (P04626) Pertuzumab FAB LIGHT CHAIN × 1 (P01834) Trastuzumab FAB LIGHT CHAIN × 1 (P01834) Trastuzumab FAB HEAVY CHAIN × 1 (Q6GMX6) ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.36 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.

105 other PDB entries and 128 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGG1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 109–222; UniProt 109–222

Trastuzumab FAB HEAVY CHAIN

Homo sapiens

UniProt Q6GMX6

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 × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 124–235 Not recorded Receptor tyrosine-protein kinase erbB-2 × 1 (P04626) Pertuzumab FAB LIGHT CHAIN × 1 (P01834) Pertuzumab FAB HEAVY CHAIN × 1 (P0DOX5) Trastuzumab FAB LIGHT CHAIN × 1 (P01834) ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.36 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.

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

View Construct and Data Evidence
UniProt name Q6GMX6_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 109–220; UniProt 124–235

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 6oge

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6oge
Deposition date deposition_date2019-04-02
Structure title titleCryo-EM structure of Her2 extracellular domain-Trastuzumab Fab-Pertuzumab Fab complex
Keywords keywordsHer2 extracellular domain, Trastuzumab, Pertuzumab, transferase-immune system complex; transferase/immune system
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.88
Radius of gyration Rg (electron density) rg_electron45.56
Forward intensity I(0) i0421211000.00
Molecular weight molecular_weight163860.0 kDa
Excluded volume excluded_volume202920 ų
Envelope volume envelope_volume302310 ų
Hydration-shell volume shell_volume56753 ų
Envelope diameter envelope_diameter140.0
Shell Rg shell_rg48.37
Envelope Rg envelope_rg44.55
Shape Rg shape_rg45.52
Total Rg total_rg45.81
Total atoms total_atoms11494
Residues n_residues1483
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 dmax144.4
Rg (real space) rg_real45.80
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real4.2120e+08
I(0) uncertainty (real space) i0_real_error7.1900e+06
Rg (reciprocal space) rg_reciprocal45.88
I(0) (reciprocal space) i0_reciprocal421300000.0000
Solution quality estimate total_estimate0.8992
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.5
Skewness Skewness skewness0.121
Kurtosis Kurtosis kurtosis-0.757
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29940000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.970; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.777

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)