7sz0

Cryo-EM structure of the extracellular module of the full-length EGFR L834R bound to EGF. "tips-juxtaposed" conformation

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Epidermal growth factor receptor

Homo sapiens

UniProt P00533

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Epidermal growth factor × 2 (P01133) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name EGFR_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1210; UniProt 1–1210 Author chain B; PDBConstruct 1–1210; UniProt 1–1210

Epidermal growth factor

Homo sapiens

UniProt P01133

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Epidermal growth factor receptor × 2 (P00533) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name EGF_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–53; UniProt 971–1023 Author chain D; PDBConstruct 1–53; UniProt 971–1023

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id7sz0
Deposition date deposition_date2021-11-25
Structure title titleCryo-EM structure of the extracellular module of the full-length EGFR L834R bound to EGF. "tips-juxtaposed" conformation
Keywords keywordsreceptor tyrosine kinases, epidermal growth factor receptor, SIGNALING PROTEIN, SIGNALING PROTEIN-RECEPTOR complex; SIGNALING PROTEIN/RECEPTOR
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

7sz0__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

7sz0__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

7sz0__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)43.93 Å
Rg (electron density)43.43 Å
Total Rg43.60 Å
Atom count10200
Residues1322
Excluded volume179700 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 7sz0__assembly_1__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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7. Citations (1)