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| [[Image:4cha.gif|left|200px]] | | {{Seed}} |
| | [[Image:4cha.png|left|200px]] |
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| {{STRUCTURE_4cha| PDB=4cha | SCENE= }} | | {{STRUCTURE_4cha| PDB=4cha | SCENE= }} |
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| '''STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION'''
| | ===STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION=== |
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| ==Overview==
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| Diffraction data for alpha-chymotrypsin crystals at -10 degrees C were measured at 1.68 A resolution and refined by restrained structure-factor least-squares refinement. The two independent chymotrypsin molecules in the crystallographic asymmetric unit were refined independently. The overall structure of alpha-chymotrypsin is little changed from published co-ordinates. The root-mean-square shift of C alpha co-ordinates is 0.42 A, co-ordinates for the two molecules showing a root-mean-square difference of 0.19 A. Certain regions with high disorder (residues 9 to 14, 73 to 79) remain difficult to interpret and several side-chains are disordered. Some water molecule positions have been changed. The absence of the tosyl group has made a significant difference to the refined structure at the active site. This now agrees closely with other enzymes of the trypsin family that have been refined at high resolution. There is a strong hydrogen bond between N epsilon 2 (His57) and O gamma (Ser195) in the free enzyme, in line with the published description of the charge relay system.
| | The line below this paragraph, {{ABSTRACT_PUBMED_4046030}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 4046030 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_4046030}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Blow, D M.]] | | [[Category: Blow, D M.]] |
| [[Category: Tsukada, H.]] | | [[Category: Tsukada, H.]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:22:07 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:32:09 2008'' |
