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PDBsum entry 1gct
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Hydrolase/peptide
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PDB id
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1gct
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Is gamma-Chymotrypsin a tetrapeptide acyl-Enzyme adduct of alpha-Chymotrypsin?
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Authors
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M.M.Dixon,
B.W.Matthews.
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Ref.
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Biochemistry, 1989,
28,
7033-7038.
[DOI no: ]
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PubMed id
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Abstract
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Refinement of the structure of gamma-chymotrypsin based on X-ray
crystallographic data to 1.6-A resolution has confirmed the overall conformation
of the molecule as reported previously [Cohen, G. H., Silverton, E. W., &
Davies, D. R. (1981) J. Mol. Biol. 148, 449-479]. In addition, the new
refinement suggests that gamma-chymotrypsin, which is operationally defined by
its crystalline habit, may not be the free enzyme but rather a complex, possibly
an acyl-enzyme adduct, with the tetrapeptide Pro-Gly-Ala-Tyr (or a close
homologue). The crystallographic refinement provides a detailed geometrical
description of the enzyme-substrate-solvent interactions that occur in the
presumptive adduct.
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Secondary reference #1
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Title
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Structure of gamma-Chymotrypsin in the range ph 2.0 to ph 10.5 suggests that gamma-Chymotrypsin is a covalent acyl-Enzyme adduct at low ph.
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Authors
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M.M.Dixon,
R.G.Brennan,
B.W.Matthews.
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Ref.
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Int J Biol Macromol, 1991,
13,
89-96.
[DOI no: ]
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PubMed id
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