Human Angiotensin converting enzyme in complex with phosphinic tripeptide

Structure

x-ray diffraction · resolution 1.97 · 1 distinct chain · 62% helix, 3% strand (DSSP).

Ligands and binding sites

• 3ES · [(2S)-2-({3-[hydroxyl(2-phenyl-(1R)-1-{[(benzyloxy)[(2s)-2-({3-[hydroxyl(2-phenyl-(1R)-1-carbonyl]-amino}ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxo-propyl}amino)-3-(4-hydroxy-phenyl) · ligand · 2 copies · chains A
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
• BMA · beta-D-mannopyranose · sugar
• FUC · alpha-L-fucopyranose · sugar · chains A
• ZN · Zinc ion · metal · chains A
• CL · Chloride ion · ion · 2 copies · chains A
• ACT · Acetate ion · additive · chains A
• EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 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, 4 with a druggability of 0.5 or more.

Modifications

Observed in the structure: 3 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

• 2XY9 · Human angiotensin converting enzyme in complex with phosphinic tripeptide · 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

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
• Elsewhere: RCSB PDB 2XY9 · PDBe 2XY9 · UniProt P12821