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: 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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