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: 18560153 DOI: 10.1107/S0907444908008561 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation