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.
Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load
and display another structure.
| load='3cin' size='350' frame='false' scene=
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| 3cin, resolution 1.70Å (default scene)
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| Ligands:
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CL, MG, NAD
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| Gene:
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TM1419, TM_1419 (Thermotoga maritima MSB8)
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| Activity:
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Inositol-3-phosphate synthase, with EC number 5.5.1.4
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| Resources:
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FirstGlance, OCA, RCSB, PDBsum, TOPSAN
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| Coordinates:
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save as pdb, mmCIF, xml
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proteopedia link