Research workbench
Crystal structures of EGFR in complex with MIG6
Analyse Crystal structures of EGFR in complex with MIG6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4R3R
- Type
- protein
- Length
- 316 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epidermal growth factor receptor; Peptide from erbb receptor feedback inhibitor 1'
- EC
- 2.7.10.1
- UniProt
- P00533, Q9UJM3
- Pockets
- 4 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epidermal growth factor receptor (EC 2.7.10.1) | protein | 309 | 38% helix, 20% strand | P00533 |
| B | Peptide from erbb receptor feedback inhibitor 1' | protein | 7 | 0% helix, 14% strand | Q9UJM3 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 348 | 0.61 | 0.77 | 42 | empty |
| 2 | 108 | 0.49 | 0.81 | 17 | empty |
| 3 | 63 | 0.37 | 0.79 | 18 | empty |
| 4 | 64 | 0.36 | 0.77 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 483 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 4R3R · Crystal structures of EGFR in complex with Mig6 · the same entry in another collection · chain A against A, TM-score 1.00
- P00533 · AlphaFold monomer V2.0 prediction for epidermal growth factor receptor (P00533) · a predicted model of the same protein · chain A against A, TM-score 0.94
- Q9UJM3 · AlphaFold monomer V2.0 prediction for erbb receptor feedback inhibitor 1 (Q9UJM3) · a predicted model of the same protein · chain B against A, TM-score 0.60
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 Q9UJM3
- Elsewhere: RCSB PDB 4R3R · PDBe 4R3R · UniProt P00533 · UniProt Q9UJM3
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