Ann Taylor sandbox 120

From Proteopedia

Revision as of 13:33, 18 February 2011 by Ann Taylor (Talk | contribs)
Jump to: navigation, search

Trypsin bound to an inhibitor

Trypsin is a serine protease. It works with a catalytic triad of aspartic acid, histidine and serine to catalyze the formation of a covalent intermediate with the substrate. There is a hydrophobic binding pocket to help align the protein with the enzyme, and an oxyanion hole to stabilize the intermediate.

Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load and display another structure.


PDB ID 1taw

Drag the structure with the mouse to rotate
1taw, resolution 1.80Å ()
Ligands:
Gene: A4 (Homo sapiens)
Activity: Trypsin, with EC number 3.4.21.4
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Proteopedia Page Contributors and Editors (what is this?)

Ann Taylor

Personal tools