Skip to main content

Table 4 Potentially novel functional sites

From: Identification of recurring protein structure microenvironments and discovery of novel functional sites around CYS residues

cluster ID Size FC Putative annotation Distinguishing features
Clust4-Sub23 5* 8.79 Structural role Extended beta sheet environment with repeated CYS flanked by PHE. * Several sites are adjacent to one another, and may be involved in disulfide bonds.
Clust5-Sub70 12 3.07 TYR phosphorylation site, possibly autocatalytic 2/3 of proteins are TYR kinases with multiple phosphorylation sites. Environment characterized by loop containing CYS, MET, and TYR.
Clust6-Sub240 5 4.33 Associated with ligand binding 80% of sites are near a bound ligand.
Clust8-Sub25 11 4.12 Structural role Inward facing CYS on a surface accessible helix surrounded by an abundance of aliphatic, hydrophobic sidechains.
Clust8-Sub352 6 4.18 Structural role Helical CYS in the vicinity of 1 HIS and several aliphatic, hydrophobic sidechains.
Clust15-Sub152 6 4.43 Associated with enzymatic activity All proteins are enzymes. Environment contains multiple ARG and occasionally HIS.
Clust21-Sub48 9* 3.06 Associated with WD repeat motif Environment characterized by beta sheets and the presence of another CYS. * Several sites are adjacent to one another.
Clust24-Sub17 5 4.34 Functional role Environment contains an ASP, a GLU, and usually at least one LYS, all charged and polar residues.
Clust25-Sub19 5 6.32 Associated with sugar kinases Beta sheet environment with multiple sulfur- containing residues.
Clust31-Sub18 5 7.00 Protein binding 80% of proteins are protein-binding. Environment characterized by helical CYS and an opposing TRP residue.
Clust36-Sub127 5 5.04 Functional role Environment is solvent exposed with an ASP and LYS forming a possible triad with the CYS.
Clust39-Sub58 5 18.34 Associated with viral proteins Sparse environment containing TRP, TYR, THR, and ARG, all polar and mostly hydrophobic residues.
  1. These predictions represent clusters where the function is not obvious but reasonable evidence exists for a coherent functional theme, even if it is in a structural role. FC = functional coherence.