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A crystal structure of EGFR(T790M/V948R) in complex with LN3754

Analyse A crystal structure of EGFR(T790M/V948R) in complex with LN3754 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WAK
Type: protein
Length: 1,209 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P00533
Ligands: ANP, TQA, MG

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D	—	protein	297	—	P00533
A	—	protein	297	—	P00533
B	—	protein	316	—	P00533
C	—	protein	299	—	P00533

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 3 copies · chains D, A, B
TQA · N-(3-{5-[2-(acetylamino)pyridin-4-yl]-2-(methylsulfanyl)-1H-imidazol-4-yl}phenyl)-2-[(1-oxo-1, 3-dihydro-2H-isoindol-2-yl)methyl]benzamide · ligand · chains C
MG · Magnesium ion · metal · 3 copies · chains D, A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6WAK · A crystal structure of EGFR(T790M/V948R) in complex with LN3754 · the same entry in another collection · chain C against C, TM-score 1.00
P00533 · AlphaFold monomer V2.0 prediction for epidermal growth factor receptor (P00533) · a predicted model of the same protein · chain C against A, TM-score 0.89

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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 6WAK · PDBe 6WAK · UniProt P00533

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