1avw
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COMPLEX PORCINE PANCREATIC TRYPSIN/SOYBEAN TRYPSIN INHIBITOR, ORTHORHOMBIC CRYSTAL FORM
OverviewOverview
The Kunitz-type trypsin inhibitor from soybean (STI) consists of 181 amino, acid residues with two disulfide bridges. Its crystal structures have been, determined in complex with porcine pancreatic trypsin in two crystal forms, (an orthorhombic form at 1.75 A resolution and a tetragonal form at 1.9 A), and in the free state at 2.3 A resolution. They have been refined to, crystallographic R-values of 18.9%, 21.6% and 19.8%, respectively. The, three models of STI reported here represent a significant improvement over, the partial inhibitor structure in the complex, which was previously, determined at a nominal resolution of 2.6 A by the multiple isomorphous, replacement method. This study provides the first high-resolution picture, of the complex between a Kunitz-type proteinase inhibitor ... [(full description)]
About this StructureAbout this Structure
1AVW is a [Protein complex] structure of sequences from [Glycine max] and [Sus scrofa] with CA as [ligand]. Active as [Trypsin], with EC number [3.4.21.4]. Structure known Active Sites: AVE and IRY. Full crystallographic information is available from [OCA].
ReferenceReference
Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator., Song HK, Suh SW, J Mol Biol. 1998 Jan 16;275(2):347-63. PMID:9466914
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