1.65 Angstrom resolution crystal structure of lmo0182 (residues 1-245) from Listeria monocytogenes EGD-e

Samuel H. Light (Contributor)
Laty A. Cahoon (Contributor)
Kiran V. Mahasenan (Contributor)
Mijoon Lee (Contributor)
Bill Boggess (Contributor)
Andrei S. Halavaty (Contributor)
Shahriar Mobashery (Contributor)
Nancy E. Freitag (Contributor)
Wayne F Anderson (Contributor)

Dataset

Date made available	Feb 1 2017
Publisher	Protein Data Bank (PDB)

DOI
10.2210/pdb5HOP/pdb

Access Dataset

https://www.wwpdb.org/pdb?id=pdb_00005hop

1 Article

Transferase Versus Hydrolase: The Role of Conformational Flexibility in Reaction Specificity
Light, S. H., Cahoon, L. A., Mahasenan, K. V., Lee, M., Boggess, B., Halavaty, A. S., Mobashery, S., Freitag, N. E. & Anderson, W. F., Feb 7 2017, In: Structure. 25, 2, p. 295-304 10 p.
Research output: Contribution to journal › Article › peer-review

Open Access
21 Scopus citations

Cite this

Light, S. H. (Contributor), Cahoon, L. A. (Contributor), Mahasenan, K. V. (Contributor), Lee, M. (Contributor), Boggess, B. (Contributor), Halavaty, A. S. (Contributor), Mobashery, S. (Contributor), Freitag, N. E. (Contributor), Anderson, W. F. (Contributor) (Feb 1 2017). 1.65 Angstrom resolution crystal structure of lmo0182 (residues 1-245) from Listeria monocytogenes EGD-e. Protein Data Bank (PDB). 10.2210/pdb5HOP/pdb

1.65 Angstrom resolution crystal structure of lmo0182 (residues 1-245) from Listeria monocytogenes EGD-e

DOI

Access Dataset

Research output

Transferase Versus Hydrolase: The Role of Conformational Flexibility in Reaction Specificity

Cite this