1wbc | pdb_00001wbc

CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES OF PSOPHOCARPIN B1, A CHYMOTRYPSIN INHIBITOR FROM WINGED BEAN SEEDS

spinqualitylabelsall models 1wbc, resolution 2.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1wbc is a 1 chain structure with sequence from Psophocarpus tetragonolobus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ICW3_PSOTE] Inhibits alpha-chymotrypsin at the molar ratio of 1:2 in state of 1:1. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Thc crystal structure of an alpha-chymotrypsin inhibitor (P6(1)22; a = 61.4, c = 210.9 A) isolated from winged bean (Psophocarpus. tetragonolobus) seeds has been determined at 2.95 A resolution by the molecular-replacement method using the 2.6 A coordinates of Erythrina trypsin inhibitor (ETI) as the starting model (57% sequence homology). This protease inhibitor, WCI, belongs to the Kunitz (STI) family and is a single polypeptide chain with 183 amino-acid residues having a molecular weight of 20 244 Da. Structure refinement with RESTRAIN and X-PLOR has led to a crystallographic R factor of 19.1% for 3469 observed reflections (I > 2sigma) in the resolution range 8-2.95 A. A total of 56 water molecules have been incorporated in the refined model containing 181 amino-acid residues. In the refined structure the deviations of bond lengths and bond angles from ideal values are 0.015 A and 2.2 degrees, respectively. The inhibitor molecule is spherical and consists of 12 antiparallel beta-strands with connecting loops arranged in a characteristic folding (a six-stranded beta-barrel and a six-stranded lid on one hollow end of the barrel) common to other homologous serine protease inhibitors in the Kunitz (STI) family as well as to some non-homologous proteins like interleukin-lalpha and interleukin-lbeta. In the structure the conformation of the protruding reactive-site loop is stabilized through hydrogen bonds mainly formed by the side chain of Asnl4, which intrudes inside the cavity of the reactive-site loop, with the side-chain and main-chain atoms of some residues in the loop region. A pseudo threefold axis exists parallel to the barrel axis of the structure. Each of the three subdomains comprises of four beta-strands with connecting loops. Structure of a Kunitz-type chymotrypsin from winged bean seeds at 2.95 A resolution.,Dattagupta JK, Podder A, Chakrabarti C, Sen U, Dutta SK, Singh M Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):521-8. PMID:15299674 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chymotrypsin inhibitor 3D structures

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