Human angiotensin-converting enzyme in complex with angiotensin-II

Structure

x-ray diffraction · 2 distinct chains · 62% helix, 4% strand (DSSP).

Ligands and binding sites

• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
• BMA · beta-D-mannopyranose · sugar
• ZN · Zinc ion · metal · chains A, P
• CL · Chloride ion · ion · 2 copies · chains A
• ACT · Acetate ion · additive · 5 copies · chains A, P
• PE4 · 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethanol · additive · 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.

Interfaces

1 interface between chains.

• A–P · 683 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide, 3 glycan (disulfide, N-glycosylation, glycosylation).

Compared structures

• 4APH · Human angiotensin-converting enzyme in complex with angiotensin-II · the same entry in another collection · chain A against A, TM-score 1.00
• P12821 · AlphaFold monomer V2.0 prediction for angiotensin-converting enzyme (P12821) · a predicted model of the same protein · chain A against A, TM-score 0.99
• P01019 · AlphaFold monomer V2.0 prediction for angiotensinogen (P01019) · a predicted model of the same protein · chain P against A, TM-score 0.60

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 P12821
• Every structure of UniProt P01019
• Elsewhere: RCSB PDB 4APH · PDBe 4APH · UniProt P12821 · UniProt P01019