1d5u | pdb_00001d5u

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MOLECULAR MODEL OF THE MATURE HUMAN CATHEPSIN F

spinqualitylabelsall models 1d5u 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, ProSAT Publication Abstract from PubMed Models of the tertiary structures of cathepsins K, S, H, and F were constructed by using homology protein modelling methods and refinements by interactive graphics and energy minimisation. The predicted structures yield information regarding their substrate binding sites and indicate the residues surrounding these sites. The ligand binding sites were characterised and compared with each other by means of calculated molecular electrostatic surface potentials. This will allow designing and development of new ligands specific for these cathepsins in future investigations. Development and validation of homology models of human cathepsins K, S, H, and F.,Fengler A, Brandt W Adv Exp Med Biol. 2000;477:255-60. PMID:10849752 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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