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EGFR L858R mutant in complex with an optimal peptide substrate

Analyse EGFR L858R mutant in complex with an optimal peptide substrate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEpidermal growth factor receptor (EC 2.7.10.1)protein31140% helix, 21% strandP00533
BPeptide substrateprotein933% helix, 33% strand—

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16440.670.7679empty
21960.520.7723empty
31180.420.7618empty

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

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