3b2h

Iodide derivative of human LFABP at high resolutionIodide derivative of human LFABP at high resolution

Structural highlights 3b2h is a 1 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: , Related: 3b2i, 3b2j, 3b2k, 3b2l, 3vg2, 3vg3, 3vg4, 3vg5, 3vg6, 3vg7 Gene: FABP1, FABPL (Homo sapiens) Resources: FirstGlance, OCA, RCSB, PDBsum Function [FABPL_HUMAN] Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. Publication Abstract from PubMed We report the use of anionic (I(-)), cationic (Ba(2+), Cd(2+)) and ionic mixtures (I(-) plus Ba(2+)) for derivatizing liver fatty acid binding protein (LFABP) crystals. Use of cationic and anionic salts in phasing experiments revealed distinct non-overlapping sites for these ions, suggesting exclusive binding regions on LFABP. Interestingly, cations of identical charge and valency (like Ba(2+) and Cd(2+)) bound to distinct pockets on the protein surface. Furthermore, a mixture of salts containing both I(-) and Ba(2+) was very useful in phasing experiments as these oppositely charged ions bound to different regions of LFABP. Our data therefore suggest that cationic and anionic salt mixtures like BaCl(2) with NH(4)I or salts like CdI, BaI where each ion has a significant anomalous signal for a given X-ray wavelength may be valuable reagents for phasing during structure determination. Utility of anion and cation combinations for phasing of protein structures.,Sharma A, Yogavel M, Sharma A J Struct Funct Genomics. 2012 May 6. PMID:22562242 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Fatty acid-binding protein

spinqualitylabelsall models 3b2h, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image