4CHA
STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION
Summary for 4CHA
| Entry DOI | 10.2210/pdb4cha/pdb |
| Descriptor | ALPHA-CHYMOTRYPSIN A, ... (4 entities in total) |
| Functional Keywords | hydrolase (serine proteinase) |
| Biological source | Bos taurus (cattle) More |
| Cellular location | Secreted, extracellular space: P00766 P00766 P00766 |
| Total number of polymer chains | 6 |
| Total formula weight | 50525.12 |
| Authors | Tsukada, H.,Blow, D.M. (deposition date: 1984-11-26, release date: 1985-04-01, Last modification date: 2024-10-23) |
| Primary citation | Tsukada, H.,Blow, D.M. Structure of alpha-chymotrypsin refined at 1.68 A resolution. J.Mol.Biol., 184:703-711, 1985 Cited by PubMed Abstract: 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. PubMed: 4046030DOI: 10.1016/0022-2836(85)90314-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.68 Å) |
Structure validation
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