Sandbox15

Subtilisin is a protease that initiates the nucleophillic attack on the peptide bond through a serine residue at the active site. It is a 275 residue globular protein with several alpha-helices and a large beta sheet. It's active site is composed of three amino acids, serine, aspartate, and histidine. This is known as a catalytic triad. Which works to break peptide bonds on polypeptides.

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spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D load='3cin' size='350' frame='false' scene=
3cin, resolution 1.70Å (default scene)
Ligands:	CL, MG, NAD
Gene:	TM1419, TM_1419 (Thermotoga maritima MSB8)
Activity:	Inositol-3-phosphate synthase, with EC number 5.5.1.4
Structural annotation: Resources: CATH : 3Cina01, 3Cina02 InterPro : Ipr016040, Ipr013021, Ipr002587 Pfam : PF07994
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum, TOPSAN
Coordinates:	save as pdb, mmCIF, xml