Structural consequences of accommodation of four non-cognate amino- acid residues in the S1 pocket of bovine trypsin and chymotrypsin

Structure

x-ray diffraction · 2 distinct chains · 12% helix, 33% strand (DSSP).

Ligands and binding sites

• CA · Calcium ion · metal · chains A
• SO4 · Sulfate ion · ion · 4 copies · chains A, I

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

Interfaces

1 interface between chains.

• A–I · 697 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

• 1P2J · Structural consequences of accommodation of four non-cognate amino-acid residues in the… · the same entry in another collection · chain I against I, TM-score 1.00
• P00974 · AlphaFold monomer V2.0 prediction for pancreatic trypsin inhibitor (P00974) · a predicted model of the same protein · chain I against A, TM-score 0.96

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 P00760
• Every structure of UniProt P00974
• Elsewhere: RCSB PDB 1P2J · PDBe 1P2J · UniProt P00760 · UniProt P00974