Research workbench
Cryo-EM structure of the extracellular module of the full-length EGFR bound to TGF-alpha "tips-separated" conformation
Analyse Cryo-EM structure of the extracellular module of the full-length EGFR bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SZ5
- Type
- protein
- Length
- 1,214 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epidermal growth factor receptor; Transforming growth factor alpha
- EC
- 2.7.10.1
- UniProt
- P00533, P01135
- Pockets
- 13 · best druggability 0.73
Structure
electron microscopy · 3 distinct chains · 7% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epidermal growth factor receptor (EC 2.7.10.1) | protein | 614 | 8% helix, 16% strand | P00533 |
| C, D | Transforming growth factor alpha | protein | 50 | 0% helix, 28% strand | P01135 |
| B | Epidermal growth factor receptor (EC 2.7.10.1) | protein | 500 | 7% helix, 19% strand | P00533 |
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 506 | 0.73 | 0.82 | 61 | empty |
| 2 | 887 | 0.73 | 0.77 | 87 | empty |
| 3 | 483 | 0.69 | 0.80 | 46 | empty |
| 4 | 373 | 0.59 | 0.76 | 30 | empty |
| 5 | 197 | 0.57 | 0.80 | 35 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1530 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 1489 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 1134 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 48 disulfide (disulfide).
Compared structures
- 7SZ5 · Cryo-EM structure of the extracellular module of the full-length EGFR bound to TGF-alpha… · the same entry in another collection · chain A against A, TM-score 1.00
- P01135 · AlphaFold monomer V2.0 prediction for protransforming growth factor alpha (P01135) · a predicted model of the same protein · chain C against A, TM-score 0.83
- P00533 · AlphaFold monomer V2.0 prediction for epidermal growth factor receptor (P00533) · a predicted model of the same protein · chain B against A, TM-score 0.64
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P00533
- Every structure of UniProt P01135
- Elsewhere: RCSB PDB 7SZ5 · PDBe 7SZ5 · UniProt P00533 · UniProt P01135
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