Protein Geometry Database: a flexible engine to explore backbone conformations and their relationships to covalent geometry

被引:30
作者
Berkholz, Donald S. [1 ]
Krenesky, Peter B. [2 ]
Davidson, John R. [2 ]
Karplus, P. Andrew [1 ]
机构
[1] Oregon State Univ, Dept Biochem & Biophys, Corvallis, OR 97331 USA
[2] Oregon State Univ, Open Source Lab, Corvallis, OR 97331 USA
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
STRUCTURE VALIDATION; BINDING-SITE; RESOLUTION; MOTIFS; RECOGNITION; REDUCTASE; STRAIN; FINDER;
D O I
10.1093/nar/gkp1013
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The backbone bond lengths, bond angles, and planarity of a protein are influenced by the backbone conformation (phi, psi), but no tool exists to explore these relationships, leaving this area as a reservoir of untapped information about protein structure and function. The Protein Geometry Database (PGD) enables biologists to easily and flexibly query information about the conformation alone, the backbone geometry alone, and the relationships between them. The capabilities the PGD provides are valuable for assessing the uniqueness of observed conformational or geometric features in protein structure as well as discovering novel features and principles of protein structure. The PGD server is available at http://pgd.science.oregonstate.edu/and the data and code underlying it are freely available to use and extend.
引用
收藏
页码:D320 / D325
页数:6
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