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The SCOP database, created by manual inspection and abetted by a battery of automated methods, aims to provide a detailed and comprehensive description of the structural and evolutionary relationships between all proteins whose structure is known.
SCOP is a (mostly) manually curated ordering of domains from the majority of proteins of known structure in a hierarchy according to structural and evolutionary relationships. Development of SCOP (version 1) concluded with SCOP 1.75, released in June 2009.
The SCOP database is built as a classification of non-redundant protein domains. A representative is selected based on its sequence (UniProtKB) and structure (PDB) and used for manual SCOP classification. The SCOP domain boundaries are assigned to both, the PDB and UniProtKB entry.
SCOP (Structural Classification of Proteins) classifies by structural and evolutionary relationships. Figure 4. CATH classification of protein folding patterns CATH classifications are available in the “Browse by Annotation” search method, as shown on the left. Three examples of different types of “Alpha Beta” domain structures are ...
The Structural Classification of Proteins (SCOP) database is a largely manual classification of protein structural domains based on similarities of their structures and amino acid sequences. A motivation for this classification is to determine the evolutionary relationship between proteins.
By providing a broad survey of protein folds and authoritative information about relatives of proteins, particularly those too ancient to be readily recognized from sequence, SCOPe is a framework for future research and classification.
The SCOP classification of protein folds. Structure analysis. Open Tree. Detailed structure analysis. How can I interactively explore the protein and DNA molecules present in the entry? Which amino acids from the protein chain participate in binding interactions with ligands? What is the build quality of the protein chain?