Sandbox88

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Caspase 7Caspase 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.

spinqualitylabelsall models PDB ID 1f1j Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1f1j, resolution 2.35Å ()
Ligands:
Non-Standard Residues:	,
Structural annotation: Resources: CATH : 1F1Ja00, 1F1Jb00 InterPro : Ipr001309, Ipr011600, Ipr016129, Ipr015917, Ipr015471, Ipr002398, Ipr002138 Pfam : PF00656 SCOP : d1f1ja_, d1f1jb_
Evolutionary conservation: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Active SiteActive 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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