6f3k

Combined solid-state NMR, solution-state NMR and EM data for structure determination of the tetrahedral aminopeptidase TET2 from P. horikoshiiCombined solid-state NMR, solution-state NMR and EM data for structure determination of the tetrahedral aminopeptidase TET2 from P. horikoshii

6f3k, resolution 4.10Å Show:Asymmetric Unit Biological Assembly Structural highlights 6f3k is a 1 chain structure with sequence from Pyrococcus horikoshii OT3. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy , Hybrid , Solid-state NMR , Solution NMR, Resolution 4.1Å Ligands: Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TET_PYRHO Functions as an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. However, can also cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. Has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity. Is involved in protein degradation, performing degradation of oligopeptides produced by the proteasome into single amino acids. See Also Aminopeptidase 3D structures