MolNFT v1 · #115137 · protein

EGFR kinase domain mutant "tmlr" with compound 29

5CAO · Epidermal growth factor receptor: “EGFR kinase domain mutant "tmlr" with compound 29”. X-ray diffraction, 1 ligand (4ZG), 3 pockets (best druggability 0.63). MolNFT v1 #115137 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 5CAO
Type: protein
Length: 300 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: 4ZG
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Epidermal growth factor receptor (EC 2.7.10.1)	protein	300	36% helix, 17% strand	P00533

Ligands and binding sites

4ZG · N~2~-[2-methyl-2-(methylsulfonyl)propyl]-N~4~-[2-methyl-1-(propan-2-yl)-1H-imidazo[4,5-c]pyridin-6-yl]pyrimidine-2,4-diamine · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	301	0.63	0.80	33	4ZG
2	137	0.58	0.83	26	empty
3	224	0.56	0.78	24	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 5CAO · PDBe 5CAO · UniProt P00533

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