Buried residues whose phosphorylation state could affect local structural conformation. The figure shows several examples of buried residues whose phosphorylation may result in conformational rearrangements, including detachment of secondary structure elements from the protein domain. Unless stated otherwise, all the structures are shown differentially colored from their amino- (cold colors) to their carboxyl-termini (hot colors), with the regions whose conformation is predicted to be affected in gray, and the phosphosites in white space-filled representation. (a) Structure of the human 7508A NBD1 domain  (Protein Data Bank [PDB]: 1xmi). (b) Structure of the autoinhibited p47phox  (PDB: 1ng2). (c) Structure of annexin-1  (PDB: 1hm6). Other residues, namely T24, S27 and S28, that can also be phosphorylated, although they are not buried, are shown in gray. The region encircled is likely to be affected by phosphorylation of the enclosed amino acids, as described in the main text. (d) Structure of the regulator of G-protein signaling 16 (unpublished data; PDB: 2bt2). (e) Structure of the serine/threonine protein phosphatase PP1-β catalytic subunit  (PDB: 1s70). A PEG molecule is shown in red and the 130 kDa myosin-binding subunit of smooth muscle myosin phosphatase in white. (f) Structure of DJ-1, a protein related to male fertility and Parkinson's disease  (PDB: 1ps4). (g) Structure of the 60S ribosomal protein L7-A  (PDB: 1s1i). (h) Structure of the elongation factor EEF1A  (PDB: 1f60), in which their individual domains are shown in blue (elongation factor Tu GTP-binding domain), cyan (elongation factor Tu domain 2), and green (elongation factor Tu carboxyl-terminal domain). The catalytic carboxyl-terminal domain of EEF1BA is shown in yellow. A list with additional details of the examples, including links to mtcPTM entries, can be found in Additional data file 2.