4cha
From Proteopedia
Line 1: | Line 1: | ||
[[Image:4cha.gif|left|200px]] | [[Image:4cha.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_4cha", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_4cha| PDB=4cha | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION''' | '''STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION''' | ||
Line 28: | Line 25: | ||
[[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 | + |
Revision as of 19:22, 4 May 2008
| |||||||||
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