3B97
Crystal Structure of human Enolase 1
Summary for 3B97
| Entry DOI | 10.2210/pdb3b97/pdb |
| Descriptor | Alpha-enolase, MAGNESIUM ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | alpha/beta hydrolase, acetylation, alternative initiation, cytoplasm, dna-binding, glycolysis, lyase, magnesium, membrane, metal-binding, nucleus, phosphorylation, plasminogen activation, polymorphism, repressor, transcription, transcription regulation |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasm. Isoform MBP-1: Nucleus: P06733 |
| Total number of polymer chains | 4 |
| Total formula weight | 188973.35 |
| Authors | Kang, H.J.,Jung, S.K.,Kim, S.J.,Chung, S.J. (deposition date: 2007-11-02, release date: 2008-09-16, Last modification date: 2024-03-13) |
| Primary citation | Kang, H.J.,Jung, S.K.,Kim, S.J.,Chung, S.J. Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme. Acta Crystallogr.,Sect.D, 64:651-657, 2008 Cited by PubMed Abstract: Aside from its enzymatic function in the glycolytic pathway, alpha-enolase (ENO1) has been implicated in numerous diseases, including metastatic cancer, autoimmune disorders, ischaemia and bacterial infection. The disease-related roles of ENO1 are mostly attributed to its immunogenic capacity, DNA-binding ability and plasmin(ogen) receptor function, which are significantly affected by its three-dimensional structure and surface properties, rather than its enzymatic activity. Here, the crystal structure of human ENO1 (hENO1) is presented at 2.2 A resolution. Despite its high sequence similarity to other enolases, the hENO1 structure exhibits distinct surface properties, explaining its various activities, including plasmin(ogen) and DNA binding. PubMed: 18560153DOI: 10.1107/S0907444908008561 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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