1abl | pdb_00001abl

HOMOLOGY MODELING OF THE ABL-SH3 DOMAIN

spinqualitylabelsall models 1abl Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum Publication Abstract from PubMed A tertiary structure model of the Abl-SH3 domain is predicted by using homology modeling techniques coupled to molecular dynamics simulations. Two template proteins were used, Fyn-SH3 and Spc-SH3. The refined model was extensively checked for errors using criteria based on stereochemistry, packing, solvation free-energy, accessible surface areas, and contact analyses. The different checking methods do not totally agree, as each one evaluates a different characteristic of protein structures. Several zones of the protein are more susceptible to incorporating errors. These include residues 13, 15, 35, 39, 45, 46, 50, and 60. An interesting finding is that the measurement of the C alpha chirality correlated well with the rest of the criteria, suggesting that this parameter might be a good indicator of correct local conformation. Deviations of more than 4 degrees may be indicative of poor local structure. Homology modeling of the Abl-SH3 domain.,Pisabarro MT, Ortiz AR, Serrano L, Wade RC Proteins. 1994 Nov;20(3):203-15. PMID:7892170 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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