Ligand-induced conformational change of insulin-regulated aminopeptidase: insights on catalytic mechanism and active site plasticity.

Structure

x-ray diffraction · 2 distinct chains.

Ligands and binding sites

• 7O2 · [(2~{S})-2-[[(2~{S})-1-azanyl-1-oxidanylidene-3-phenyl-propan-2-yl]carbamoyl]-4,4-diphenyl-butyl]-[(1~{R})-1-azanyl-3-phenyl-propyl]phosphinic acid · ligand · 2 copies · chains A, B
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 44 copies · chains A, B
• BMA · beta-D-mannopyranose · sugar · 9 copies · chains A, B
• MAN · alpha-D-mannopyranose · sugar · 6 copies · chains A
• ZN · Zinc ion · metal · 2 copies · chains A, B
• BR · Bromide ion · ion · 21 copies · chains A, B

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

Compared structures

• 5MJ6 · Ligand-induced conformational change of Insulin-regulated aminopeptidase: insights on… · the same entry in another collection · chain A against A, TM-score 1.00
• Q9UIQ6 · AlphaFold monomer V2.0 prediction for leucyl-cystinyl aminopeptidase (Q9UIQ6) · a predicted model of the same protein · chain B 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 Q9UIQ6
• Elsewhere: RCSB PDB 5MJ6 · PDBe 5MJ6 · UniProt Q9UIQ6