1GBC
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID
Summary for 1GBC
| Entry DOI | 10.2210/pdb1gbc/pdb |
| Related PRD ID | PRD_000317 |
| Descriptor | ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID INHIBITOR, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | active-site mutation, serine proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Lysobacter enzymogenes |
| Total number of polymer chains | 2 |
| Total formula weight | 20505.52 |
| Authors | Mace, J.E.,Agard, D.A. (deposition date: 1995-09-06, release date: 1996-01-29, Last modification date: 2021-11-03) |
| Primary citation | Mace, J.E.,Agard, D.A. Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J.Mol.Biol., 254:720-736, 1995 Cited by PubMed: 7500345DOI: 10.1006/jmbi.1995.0650 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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