1uhb
From Proteopedia
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| , resolution 2.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of porcine alpha trypsin bound with auto catalyticaly produced native peptide at 2.15 A resolution
Overview
Trypsin, a serine protease enzyme plays a pivotal role in digestion and is autocatalytic. The crystal structure of a complex formed between porcine trypsin and an auto catalytically produced peptide is reported here. This complex shows a reduction in enzyme activity as compared to native beta-trypsin. The nonapeptide has a lysine, which is recognized by Asp 189 at the specificity pocket. The auto catalytically produced native nonapeptide is bound at the active site cleft like other trypsin inhibitors but the important interactions with the oxyanion hole are absent. The peptide covers only a part of the active site cleft and hence the enzyme activity is reduced rather than being inhibited.
About this Structure
1UHB is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Trypsin activity reduced by an autocatalytically produced nonapeptide., Ibrahim BS, Shamaladevi N, Pattabhi V, J Biomol Struct Dyn. 2004 Jun;21(6):737-44. PMID:15106996
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