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EGFR kinase domain with compound 41A

Analyse EGFR kinase domain with compound 41A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CAV
Type: protein
Length: 306 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: 4ZQ
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Epidermal growth factor receptor (EC 2.7.10.1)	protein	306	38% helix, 19% strand	P00533

Ligands and binding sites

4ZQ · (1R)-1-{6-({2-[(3R,4S)-3-fluoro-4-methoxypiperidin-1-yl]pyrimidin-4-yl}amino)-1-[(2S)-1,1,1-trifluoropropan-2-yl]-1H-imidazo[4,5-c]pyridin-2-yl}ethanol · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	488	0.65	0.77	56	4ZQ
2	236	0.64	0.82	32	empty
3	77	0.43	0.80	19	empty

Compared structures

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 5CAV · PDBe 5CAV · UniProt P00533

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