3b97 | pdb_00003b97

Crystal Structure of human Enolase 1

spinqualitylabelsall models 3b97, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3b97 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, SO4 Activity: Phosphopyruvate hydratase, with EC number 4.2.1.11 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ENOA_HUMAN] Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production. MBP1 binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme.,Kang HJ, Jung SK, Kim SJ, Chung SJ Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):651-7. Epub 2008, May 14. PMID:18560153 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Enolase 3D structures

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