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This sandbox is in use until August 1, 2011 for UMass Chemistry 423. Others please do not edit this page. Thanks!



Caspase 7

This is the structure for Caspase 7 with substrate bound. Caspase 7 is a Cysteine dependent protease that cleaves after ASPartate residues. The substrate here is the peptide DEVD. Caspase 7 plays a critical role in apoptosis as an initiator that cleaves downstream targets.

All caspases are zymogens. In the case of Casp7, this means that there is a prodomain that, when attached, renders the protein inactive. However, this prodomain is easily cleaved off, thus activating Casp7 as a protease.


PDB ID 1f1j

Drag the structure with the mouse to rotate
1f1j, resolution 2.35Å ()
Ligands:
Non-Standard Residues: ,
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Active Site

The active site for Caspase 7 takes full advantage of acid base chemistry. Histidine 144 will act as a base, pulling the hydrogen away from cysteine 186. This will make that cysteine very nucleophilic and thus very active. It will bind substrate and cleave after an aspartate residue.

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