Assignment of pterin deaminase activity to an enzyme of unknown function guided by homology modeling and docking.

ABSTRACT: Of the over 22 million protein sequences in the nonredundant TrEMBL database, fewer than 1% have experimentally confirmed functions. Structure-based methods have been used to predict enzyme activities from experimentally determined structures; however, for the vast majority of proteins, no such structures are available. Here, homology models of a functionally uncharacterized amidohydrolase from Agrobacterium radiobacter K84 (Arad3529) were computed on the basis of a remote template structure. The protein backbone of two loops near the active site was remodeled, resulting in four distinct active site conformations. Substrates of Arad3529 were predicted by docking of 57,672 high-energy intermediate (HEI) forms of 6440 metabolites against these four homology models. On the basis of docking ra

SUBMITTER: Fan H 

PROVIDER: S-EPMC3557803 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature