The active site of the SGNH hydrolase-like fold proteins: Nucleophile–oxyanion (Nuc-Oxy) and Acid–Base zones
Open Access
- 29 December 2023
- journal article
- research article
- Published by Elsevier in Current Research in Structural Biology
- Vol. 7, 100123
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functionsNucleic Acids Research, 2012
- Structural and Biochemical Characterization of the Salicylyl-acyltranferase SsfX3 from a Tetracycline Biosynthetic PathwayJournal of Biological Chemistry, 2011
- Structural and enzymatic characterization of NanS (YjhS), a 9‐O‐Acetyl N‐acetylneuraminic acid esterase from Escherichia coli O157:H7Protein Science, 2011
- Inference of Macromolecular Assemblies from Crystalline StateJournal of Molecular Biology, 2007
- Mimicry by asx‐ and ST‐turns of the four main types of β‐turn in proteinsProtein Science, 2004
- The Protein Data BankNucleic Acids Research, 2000
- A recurring two-hydrogen-bond motif incorporating A serine or threonine residue is found both at α-helical N termini and in other situations 1 1Edited by J. M. ThorntonJournal of Molecular Biology, 1999
- A natural grouping of motifs with an aspartate or asparagine residue forming two hydrogen bonds to residues ahead in sequence: their occurrence at α-helical N termini and in other situations 1 1Edited by J. M. ThorntonJournal of Molecular Biology, 1999
- A new family of lipolytic enzymes?Trends in Biochemical Sciences, 1995
- MOLSCRIPT: a program to produce both detailed and schematic plots of protein structuresJournal of Applied Crystallography, 1991