Two “unrelated” families of ATP-dependent enzymes share extensive structural similarities about their cofactor binding sites
- 1 May 1998
- journal article
- research article
- Published by Wiley in Protein Science
- Vol. 7 (5) , 1136-1146
- https://doi.org/10.1002/pro.5560070507
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- ATP binding proteins with different folds share a common ATP-binding structural motifNature Structural & Molecular Biology, 1997
- Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteinsProtein Engineering, Design and Selection, 1996
- Structural classification of proteins: new superfamiliesCurrent Opinion in Structural Biology, 1996
- Improved genetic algorithm-based protein structure comparisons: pairwise and multiple superpositionsProtein Engineering, Design and Selection, 1995
- Three-Dimensional Structure of the Biotin Carboxylase Subunit of Acetyl-CoA CarboxylaseBiochemistry, 1994
- Protein structure comparisons using a combination of a genetic algorithm, dynamic programming and least-squares minimizationProtein Engineering, Design and Selection, 1994
- Three-dimensional Structure of the Glutathione Synthetase from Escherichia coli B at 2·0 Å ResolutionJournal of Molecular Biology, 1993
- MOLSCRIPT: a program to produce both detailed and schematic plots of protein structuresJournal of Applied Crystallography, 1991
- The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic DomainsScience, 1988
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977