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Crystal structure of EGFR kinase domain G719S mutation in complex with iressa

Analyse Crystal structure of EGFR kinase domain G719S mutation in complex with iressa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ITO
Type: protein
Length: 303 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Epidermal growth factor receptor
EC: 2.7.10.1
UniProt: P00533
Ligands: IRE
Pockets: 4 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Epidermal growth factor receptor (EC 2.7.10.1)	protein	303	37% helix, 17% strand	P00533

Ligands and binding sites

IRE · Gefitinib · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	418	0.66	0.79	45	IRE
2	130	0.46	0.77	18	empty
3	106	0.41	0.76	20	empty
4	108	0.40	0.76	21	empty

Compared structures

2ITO · Crystal structure of EGFR kinase domain G719S mutation in complex with Iressa · 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 0.95

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 2ITO · PDBe 2ITO · UniProt P00533

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