1JEN
HUMAN S-ADENOSYLMETHIONINE DECARBOXYLASE
Summary for 1JEN
| Entry DOI | 10.2210/pdb1jen/pdb |
| Descriptor | PROTEIN (S-ADENOSYLMETHIONINE DECARBOXYLASE (BETA CHAIN)), PROTEIN (S-ADENOSYLMETHIONINE DECARBOXYLASE (ALPHA CHAIN)) (3 entities in total) |
| Functional Keywords | s-adenosylmethionine decarboxylase, pyruvoyl, gene duplication, polyamine biosynthesis, sandwich, allosteric enzyme |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 76933.36 |
| Authors | Ekstrom, J.L.,Mathews, I.I.,Stanley, B.A.,Pegg, A.E.,Ealick, S.E. (deposition date: 1999-02-23, release date: 1999-06-01, Last modification date: 2024-11-13) |
| Primary citation | Ekstrom, J.L.,Mathews, I.I.,Stanley, B.A.,Pegg, A.E.,Ealick, S.E. The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold. Structure Fold.Des., 7:583-595, 1999 Cited by PubMed Abstract: S-Adenosylmethionine decarboxylase (AdoMetDC) is a critical regulatory enzyme of the polyamine synthetic pathway, and a well-studied drug target. The AdoMetDC decarboxylation reaction depends upon a pyruvoyl cofactor generated via an intramolecular proenzyme self-cleavage reaction. Both the proenzyme-processing and substrate-decarboxylation reactions are allosterically enhanced by putrescine. Structural elucidation of this enzyme is necessary to fully interpret the existing mutational and inhibitor-binding data, and to suggest further experimental studies. PubMed: 10378277DOI: 10.1016/S0969-2126(99)80074-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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