2RG3
Covalent complex structure of elastase
Summary for 2RG3
| Entry DOI | 10.2210/pdb2rg3/pdb |
| Related | 1ppg |
| Descriptor | Leukocyte elastase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (4 entities in total) |
| Functional Keywords | elastase, complex, covalent, disease mutation, glycoprotein, hydrolase, protease, serine protease, zymogen |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 24334.09 |
| Authors | Huang, W.,Yamamoto, Y. (deposition date: 2007-10-02, release date: 2008-07-01, Last modification date: 2020-07-29) |
| Primary citation | Huang, W.,Yamamoto, Y.,Li, Y.,Dou, D.,Alliston, K.R.,Hanzlik, R.P.,Williams, T.D.,Groutas, W.C. X-ray snapshot of the mechanism of inactivation of human neutrophil elastase by 1,2,5-thiadiazolidin-3-one 1,1-dioxide derivatives. J.Med.Chem., 51:2003-2008, 2008 Cited by PubMed Abstract: The mechanism of action of a general class of mechanism-based inhibitors of serine proteases, including human neutrophil elastase (HNE), has been elucidated by determining the X-ray crystal structure of an enzyme-inhibitor complex. The captured intermediate indicates that processing of inhibitor by the enzyme generates an N-sulfonyl imine functionality that is tethered to Ser195, in accordance with the postulated mechanism of action of this class of inhibitors. The identity of the HNE-N-sulfonyl imine species was further corroborated using electrospray ionization mass spectrometry. PubMed: 18318470DOI: 10.1021/jm700966p PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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