Structure and mechanism of MT-ADPRase, a nudix hydrolase from Mycobacterium tuberculosis. [electronic resource]
Producer: 20040414Description: 1015-23 p. digitalISSN:- 0969-2126
- Adenosine Diphosphate Ribose -- metabolism
- Amino Acid Sequence
- Binding Sites
- Catalysis
- Crystallography, X-Ray
- Dimerization
- Enzyme Activation
- Escherichia coli -- enzymology
- Gadolinium -- metabolism
- Helix-Loop-Helix Motifs
- Humans
- Hydrogen Bonding
- Hydrolases -- chemistry
- Ligands
- Manganese -- metabolism
- Models, Molecular
- Molecular Sequence Data
- Molecular Structure
- Mycobacterium tuberculosis -- enzymology
- Protein Conformation
- Protein Structure, Tertiary
- Pyrophosphatases -- chemistry
- Sequence Homology, Amino Acid
- Species Specificity
- Substrate Specificity
- Water -- chemistry
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Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
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