Structure of the complex between bovine alpha-chymotrypsin and pmp-C, an inhibitor from the insect locusta migratoria

Structure

x-ray diffraction · 3 distinct chains · 8% helix, 35% strand (DSSP).

Ligands and binding sites

• CD · Cadmium ion · metal · 6 copies · chains A, B, C

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• A–I · 824 Ų buried · 13 hydrogen bonds · protein-protein
• C–K · 790 Ų buried · 11 hydrogen bonds · protein-protein
• B–J · 773 Ų buried · 10 hydrogen bonds · protein-protein
• A–C · 208 Ų buried · 1 hydrogen bond · protein-protein
• A–B · 191 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 24 disulfide (disulfide).

Compared structures

• 1GL1 · structure of the complex between bovine alpha-chymotrypsin and PMP-C, an inhibitor from… · the same entry in another collection · chain C against C, TM-score 1.00
• P00766 · AlphaFold monomer V2.0 prediction for chymotrypsinogen a (P00766) · a predicted model of the same protein · chain C against A, TM-score 0.99
• P80060 · AlphaFold monomer V2.0 prediction for protease inhibitors (P80060) · a predicted model of the same protein · chain J 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 P00766
• Every structure of UniProt P80060
• Elsewhere: RCSB PDB 1GL1 · PDBe 1GL1 · UniProt P00766 · UniProt P80060