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4cha

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[[Image:4cha.gif|left|200px]]
[[Image:4cha.gif|left|200px]]
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{{Structure
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|PDB= 4cha |SIZE=350|CAPTION= <scene name='initialview01'>4cha</scene>, resolution 1.68&Aring;
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] </span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cha OCA], [http://www.ebi.ac.uk/pdbsum/4cha PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=4cha RCSB]</span>
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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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[[Category: Blow, D M.]]
[[Category: Blow, D M.]]
[[Category: Tsukada, H.]]
[[Category: Tsukada, H.]]
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[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:22:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:38:15 2008''
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Revision as of 19:22, 4 May 2008

Image:4cha.gif


PDB ID 4cha

Drag the structure with the mouse to rotate
4cha, resolution 1.68Å ()
Activity: Chymotrypsin, with EC number 3.4.21.1
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION


Overview

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.

About this Structure

4CHA is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

Structure of alpha-chymotrypsin refined at 1.68 A resolution., Tsukada H, Blow DM, J Mol Biol. 1985 Aug 20;184(4):703-11. PMID:4046030 Page seeded by OCA on Sun May 4 22:22:07 2008

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