 |
|
PDBe Entry: 1gbe
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU
|
||||||||||||||||||||||||||||||||||||||||||||||||||
| Summary | |
|||||||||||||
| Header |
HYDROLASE (SERINE PROTEINASE)
|
|||||||||||||
| Method | X-RAY DIFFRACTION | |||||||||||||
| Experiment | Resolution: 2.3 Å, R-factor: 14.1%, Spacegroup: P 32 2 1 | |||||||||||||
| Released | 29/01/1996, deposition: 06/09/1995, last revision: 24/02/2009 | |||||||||||||
| Authors |
Mace, J.E.; Agard, D.A.
|
|||||||||||||
| Primary citation |
Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J.MOL.BIOL. vol:254, pag:720-736 (1995) [PubMed ID 7500345 ]
|
|||||||||||||
| Keywords |
ACTIVE-SITE MUTATION, HYDROLASE (SERINE PROTEINASE)
|
|||||||||||||
| EC |
3.4.21.12 ExPASy BRENDA (A)
|
|||||||||||||
| Organism |
Lysobacter enzymogenes 69(A)
|
|||||||||||||
| UniProt |
Alpha-lytic protease precursor (EC 3.4.21.12) (Alpha-lytic endopeptidase) P00778 (A)
|
|||||||||||||
| Solvent | A | |||||||||||||
| Polymers |
|
|||||||||||||
| Heterogens |
|
|||||||||||||