4cha: Difference between revisions
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[[Image:4cha.gif|left|200px]] | [[Image:4cha.gif|left|200px]] | ||
'''STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION''' | {{Structure | ||
|PDB= 4cha |SIZE=350|CAPTION= <scene name='initialview01'>4cha</scene>, resolution 1.68Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
4CHA is a [ | 4CHA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHA OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/4046030 4046030] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Chymotrypsin]] | [[Category: Chymotrypsin]] | ||
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[[Category: hydrolase (serine proteinase)]] | [[Category: hydrolase (serine proteinase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:09:16 2008'' | ||
Revision as of 17:09, 20 March 2008
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| 4cha, resolution 1.68Å | |||||||||||||
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| Activity: | Chymotrypsin, with EC number 3.4.21.1 | ||||||||||||
| 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 Thu Mar 20 19:09:16 2008
