Ascaris suum carboxypeptidase inhibitor in complex with human carboxypeptidase A1

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 18% strand (DSSP).

Ligands and binding sites

• ZN · Zinc ion · metal · 10 copies · chains A, B
• NA · Sodium ion · metal · chains A
• ACT · Acetate ion · additive · 6 copies · chains A, B
• CAC · Cacodylate ion · additive · 4 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 722 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

• 3FJU · Ascaris suum carboxypeptidase inhibitor in complex with human carboxypeptidase A1 · the same entry in another collection · chain A against A, TM-score 1.00
• P15085 · AlphaFold monomer V2.0 prediction for carboxypeptidase A1 (P15085) · a predicted model of the same protein · chain A against A, TM-score 1.00
• P19399 · AlphaFold monomer V2.0 prediction for carboxypeptidase a inhibitor (P19399) · a predicted model of the same protein · chain B against A, TM-score 0.89

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 P15085
• Every structure of UniProt P19399
• Elsewhere: RCSB PDB 3FJU · PDBe 3FJU · UniProt P15085 · UniProt P19399