1rl7

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

MODEL STRUCTURE OF SP1 (STABLE PROTEIN 1) FROM ASPEN PLANTMODEL STRUCTURE OF SP1 (STABLE PROTEIN 1) FROM ASPEN PLANT

Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed A three dimensional theoretical model of SP1 (stable protein 1), which is resistant to high temperature and biotic-stresses, is presented here. The model was generated by the application of homology modeling technique. The conformational rigidity imparted to the fold by the presence of hydrogen-bonded, C5, C7, C10 and C13 structures in the loop regions, multiple aromatic--aromatic interactions at the protein interior and on the surface, in addition to salt-links and hydrogen-bonds are primarily the major factors, responsible for the increased stability of protein. The putative protein family is characterized by motifs, E-x(0,1)-L-x-[AEGQS] and V-x(2,3)-L-x-[ADEGST] and the active site in the tertiary structure is formed by conserved aromatic and isoleucine clusters. Structural features in the model of a thermostable and stress-resistant protein, SP1 from aspen.,Rathore RS, Narasimhamurthy T J Biomol Struct Dyn. 2004 Apr;21(5):651-5. PMID:14769057 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1rl7 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image