Crystal structure of human epidermal growth factor receptor (residues 1-501) in complex with TGF-alpha

Structure

x-ray diffraction · 4 distinct chains · 12% helix, 26% strand (DSSP).

Ligands and binding sites

• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A, B
• FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A, B
• BMA · beta-D-mannopyranose · sugar · 2 copies · chains A
• MAN · alpha-D-mannopyranose · sugar · chains A
• CD · Cadmium ion · metal · 11 copies · chains A, B, C, D
• PT · Platinum (II) ion · metal · 7 copies · chains A, B
• CL · Chloride ion · ion · 4 copies · chains A, B

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

Pockets

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

Interfaces

3 interfaces between chains.

• B–D · 1542 Ų buried · 21 hydrogen bonds · protein-protein
• A–C · 1477 Ų buried · 23 hydrogen bonds · protein-protein
• A–B · 1159 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 40 disulfide, 5 glycan (disulfide, N-glycosylation).

Compared structures

• 1MOX · Crystal Structure of Human Epidermal Growth Factor Receptor (residues 1-501) in complex… · the same entry in another collection · chain D against D, TM-score 1.00
• P01135 · AlphaFold monomer V2.0 prediction for protransforming growth factor alpha (P01135) · a predicted model of the same protein · chain D against A, TM-score 0.83
• 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 0.64

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
• Every structure of UniProt P01135
• Elsewhere: RCSB PDB 1MOX · PDBe 1MOX · UniProt P00533 · UniProt P01135