On the disordered activation domain in trypsinogen. chemical labelling and low-temperature crystallography

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 34% strand (DSSP).

Ligands and binding sites

• CA · Calcium ion · metal · chains A
• MOH · Methanol · additive · 2 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, 1 with a druggability of 0.5 or more.

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

• 2TGT · On the disordered activation domain in trypsinogen. chemical labelling and… · the same entry in another collection · chain A against A, TM-score 1.00
• 1TNL · Prediction of novel serine protease inhibitors · a predicted model of the same protein · chain A against A, TM-score 0.98
• 1TNI · Prediction of novel serine protease inhibitors · a predicted model of the same protein · chain A against A, TM-score 0.98
• 1TNJ · Prediction of novel serine protease inhibitors · a predicted model of the same protein · chain A against A, TM-score 0.98
• 1TNK · Prediction of novel serine protease inhibitors · a predicted model of the same protein · chain A against A, TM-score 0.98
• 1TNH · Prediction of novel serine protease inhibitors · a predicted model of the same protein · chain A against A, TM-score 0.98
• 1TNG · Prediction of novel serine protease inhibitors · a predicted model of the same protein · chain A against A, TM-score 0.98

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
• Elsewhere: RCSB PDB 2TGT · PDBe 2TGT · UniProt P00760