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1MCT

THE REFINED 1.6 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN PORCINE BETA-TRYPSIN AND MCTI-A, A TRYPSIN INHIBITOR OF SQUASH FAMILY

Summary for 1MCT
Entry DOI10.2210/pdb1mct/pdb
DescriptorBETA-TRYPSIN, TRYPSIN INHIBITOR A, CALCIUM ION, ... (4 entities in total)
Functional Keywordshydrolase-hydrolase inhibitor complex, proteinase, hydrolase/hydrolase inhibitor
Biological sourceSus scrofa (pig)
More
Cellular locationSecreted, extracellular space: P00761
Secreted: P30709
Total number of polymer chains2
Total formula weight26695.43
Authors
Huang, Q.,Liu, S.,Tang, Y. (deposition date: 1992-10-24, release date: 1994-01-31, Last modification date: 2024-10-30)
Primary citationHuang, Q.,Liu, S.,Tang, Y.
Refined 1.6 A resolution crystal structure of the complex formed between porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex.
J.Mol.Biol., 229:1022-1036, 1993
Cited by
PubMed Abstract: The crystal structure of the complex formed by porcine beta-trypsin with the MCTI-A inhibitor (Momordica charantia, Linn. Cucurbitaceae) has been determined at 1.6 A resolution using the molecular replacement method. The sequence of MCTI-A was determined by recognizing the electron density, and shows that MCTI-A is a member of the squash family of trypsin inhibitors. We report the first high-resolution structure of porcine beta-trypsin. Detailed comparisons have been made on the overall structure, solvent structure and active-site geometries between this complex and bovine beta-trypsin and its complexes. On the basis of our results, we discuss the interaction patterns between inhibitor and trypsin. Unlike other complex structures formed by bovine trypsin with inhibitors, no out-of-plane distortion around the inhibitor's scissible peptide was observed. The role of the trypsin catalytic triad is also discussed on the basis of this structure.
PubMed: 8445634
DOI: 10.1006/jmbi.1993.1102
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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数据于2025-06-18公开中

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