1P10
STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES
Summary for 1P10
Entry DOI | 10.2210/pdb1p10/pdb |
Related PRD ID | PRD_000316 |
Descriptor | ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-VALINE BORONIC ACID INHIBITOR, SULFATE ION, ... (4 entities in total) |
Functional Keywords | serine proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Lysobacter enzymogenes |
Total number of polymer chains | 2 |
Total formula weight | 20381.40 |
Authors | Bone, R.,Agard, D.A. (deposition date: 1989-04-24, release date: 1990-04-15, Last modification date: 2012-12-12) |
Primary citation | Bone, R.,Silen, J.L.,Agard, D.A. Structural plasticity broadens the specificity of an engineered protease. Nature, 339:191-195, 1989 Cited by PubMed: 2716847DOI: 10.1038/339191a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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