MolNFT v1 · #115972 · protein
EGFR L858R mutant in complex with an optimal peptide substrate
5CZH · Epidermal growth factor receptor: “EGFR L858R mutant in complex with an optimal peptide substrate”. X-ray diffraction, 3 pockets (best druggability 0.67). MolNFT v1 #115972 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5CZH
- Type
- protein
- Length
- 320 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epidermal growth factor receptor; Peptide substrate
- EC
- 2.7.10.1
- UniProt
- P00533
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epidermal growth factor receptor (EC 2.7.10.1) | protein | 311 | 40% helix, 21% strand | P00533 |
| B | Peptide substrate | protein | 9 | 33% helix, 33% strand | — |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 644 | 0.67 | 0.76 | 79 | empty |
| 2 | 196 | 0.52 | 0.77 | 23 | empty |
| 3 | 118 | 0.42 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 501 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 5CZH · EGFR L858R mutant in complex with an optimal peptide substrate · 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
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
- Elsewhere: RCSB PDB 5CZH · PDBe 5CZH · UniProt P00533
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