2H5D
0.9A resolution crystal structure of alpha-lytic protease complexed with a transition state analogue, MeOSuc-Ala-Ala-Pro-Val boronic acid
Summary for 2H5D
| Entry DOI | 10.2210/pdb2h5d/pdb |
| Related | 1P03 1QRX 1SSX 1TAL 2H5C 2ULL |
| Related PRD ID | PRD_000316 |
| Descriptor | ALPHA-LYTIC PROTEASE, MEOSUC-ALA-ALA-PRO-ALA BORONIC ACID INHIBITOR, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | a-lytic protease, serine protease, acylation transition state, catalysis, protein folding, protein stability, packing distortion, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Lysobacter enzymogenes |
| Total number of polymer chains | 2 |
| Total formula weight | 21206.05 |
| Authors | Fuhrmann, C.N.,Agard, D.A. (deposition date: 2006-05-25, release date: 2006-09-26, Last modification date: 2023-11-15) |
| Primary citation | Fuhrmann, C.N.,Daugherty, M.D.,Agard, D.A. Subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis J.Am.Chem.Soc., 128:9086-9102, 2006 Cited by PubMed: 16834383DOI: 10.1021/ja057721o PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.9 Å) |
Structure validation
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