2ACO
Xray structure of Blc dimer in complex with vaccenic acid
Summary for 2ACO
Entry DOI | 10.2210/pdb2aco/pdb |
Related | 1QWD |
Descriptor | Outer membrane lipoprotein blc, VACCENIC ACID (3 entities in total) |
Functional Keywords | lipocalin, fatty acid, e.coli, lipid transport, membrane protein |
Biological source | Escherichia coli |
Cellular location | Cell outer membrane; Lipid-anchor: P0A901 |
Total number of polymer chains | 2 |
Total formula weight | 39854.86 |
Authors | Campanacci, V.,Bishop, R.E.,Reese, L.,Blangy, S.,Tegoni, M.,Cambillau, C. (deposition date: 2005-07-19, release date: 2006-08-01, Last modification date: 2023-08-23) |
Primary citation | Campanacci, V.,Bishop, R.E.,Blangy, S.,Tegoni, M.,Cambillau, C. The membrane bound bacterial lipocalin Blc is a functional dimer with binding preference for lysophospholipids. Febs Lett., 580:4877-4883, 2006 Cited by PubMed: 16920109DOI: 10.1016/j.febslet.2006.07.086 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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