4cha
From Proteopedia
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| - | [[Image:4cha.gif|left|200px]] | + | [[Image:4cha.gif|left|200px]] |
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| - | '''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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| , resolution 1.68Å | |||||||
|---|---|---|---|---|---|---|---|
| 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
