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HOMSTRAD: A database of protein structure alignments for homologous families
Author(s) -
Mizuguchi Kenji,
Deane Charlotte M.,
Blundell Tom L.,
Overington John P.
Publication year - 1998
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560071126
Subject(s) - database , protein structure database , computer science , set (abstract data type) , protein structure , protein family , interface (matter) , protein superfamily , sequence alignment , amino acid residue , information retrieval , data mining , biology , peptide sequence , sequence database , genetics , programming language , biochemistry , bubble , maximum bubble pressure method , parallel computing , gene
We describe a database of protein structure alignments for homologous families. The database HOMSTRAD presently contains 130 protein families and 590 aligned structures, which have been selected on the basis of quality of the X-ray analysis and accuracy of the structure. For each family, the database provides a structure-based alignment derived using COMPARER and annotated with JOY in a special format that represents the local structural environment of each amino acid residue. HOMSTRAD also provides a set of superposed atomic coordinates obtained using MNYFIT, which can be viewed with a graphical user interface or used for comparative modeling studies. The database is freely available on the World Wide Web at: http://www-cryst.bioc.cam. ac.uk/-homstrad/, with search facilities and links to other databases.