1UHB

Crystal structure of porcine alpha trypsin bound with auto catalyticaly produced native peptide at 2.15 A resolution

Summary for 1UHB

• Entry DOI: 10.2210/pdb1uhb/pdb
• Related: 1qqu
• Descriptor: Trypsin, 9-mer peptide from Trypsin, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: serine protease, hydrolase, peptide trypsin complex
• Biological source: Sus scrofa (pig); More
• Total number of polymer chains: 3
• Total formula weight: 24507.51

Authors

Pattabhi, V.,Syed Ibrahim, B.,Shamaladevi, N. (deposition date: 2003-06-27, release date: 2004-07-27, Last modification date: 2023-10-25)

Primary citation

Ibrahim, B.S.,Shamaladevi, N.,Pattabhi, V.
Trypsin activity reduced by an autocatalytically produced nonapeptide.
J.Biomol.Struct.Dyn., 21:737-744, 2004

PubMed Abstract: 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.

PubMed: 15106996
DOI: 10.1080/07391102.2004.10506964

Experimental method

X-RAY DIFFRACTION (2.15 Å)