1OXG

Crystal structure of a complex formed between organic solvent treated bovine alpha-chymotrypsin and its autocatalytically produced highly potent 14-residue peptide at 2.2 resolution

Summary for 1OXG

• Entry DOI: 10.2210/pdb1oxg/pdb
• Related: 1ACB 4CHA 6CHA
• Descriptor: Chymotrypsinogen A, SULFATE ION, ... (4 entities in total)
• Functional Keywords: autocatalysis, organic solvent treatment, inhibition, hydrolase
• Biological source: Bos taurus (bovine); More
• Cellular location: Secreted, extracellular space: P00766 P00766
• Total number of polymer chains: 2
• Total formula weight: 27803.09

Authors

Singh, N.,Jabeen, T.,Sharma, S.,Roy, I.,Gupta, M.N.,Bilgrami, S.,Singh, T.P. (deposition date: 2003-04-02, release date: 2004-05-18, Last modification date: 2023-10-25)

• Primary citation: Singh, N.,Jabeen, T.,Sharma, S.,Roy, I.,Gupta, M.N.,Bilgrami, S.,Somvanshi, R.K.,Dey, S.,Perbandt, M.,Betzel, C.,Srinivasan, A.,Singh, T.P.; Detection of native peptides as potent inhibitors of enzymes. Crystal structure of the complex formed between treated bovine alpha-chymotrypsin and an autocatalytically produced fragment, IIe-Val-Asn-Gly-Glu-Glu-Ala-Val-Pro-Gly-Ser-Trp-Pro-Trp, at 2.2 angstroms resolution.; Febs J., 272:562-572, 2005; PubMed: 15654893; DOI: 10.1111/j.1742-4658.2004.04499.x

Experimental method

X-RAY DIFFRACTION (2.2 Å)