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Atomistry » Manganese » PDB 1n0n-1o99 » 1n2h | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 1n0n-1o99 » 1n2h » |
Manganese in PDB 1n2h: Crystal Structure of A Pantothenate Synthetase From M. Tuberculosis in Complex with A Reaction Intermediate, Pantoyl AdenylateEnzymatic activity of Crystal Structure of A Pantothenate Synthetase From M. Tuberculosis in Complex with A Reaction Intermediate, Pantoyl Adenylate
All present enzymatic activity of Crystal Structure of A Pantothenate Synthetase From M. Tuberculosis in Complex with A Reaction Intermediate, Pantoyl Adenylate:
6.3.2.1; Protein crystallography data
The structure of Crystal Structure of A Pantothenate Synthetase From M. Tuberculosis in Complex with A Reaction Intermediate, Pantoyl Adenylate, PDB code: 1n2h
was solved by
S.Wang,
D.Eisenberg,
Tb Structural Genomics Consortium (Tbsgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Manganese Binding Sites:
The binding sites of Manganese atom in the Crystal Structure of A Pantothenate Synthetase From M. Tuberculosis in Complex with A Reaction Intermediate, Pantoyl Adenylate
(pdb code 1n2h). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of A Pantothenate Synthetase From M. Tuberculosis in Complex with A Reaction Intermediate, Pantoyl Adenylate, PDB code: 1n2h: Manganese binding site 1 out of 1 in 1n2hGo back to Manganese Binding Sites List in 1n2h
Manganese binding site 1 out
of 1 in the Crystal Structure of A Pantothenate Synthetase From M. Tuberculosis in Complex with A Reaction Intermediate, Pantoyl Adenylate
Mono view Stereo pair view
Reference:
S.Wang,
D.Eisenberg.
Crystal Structures of A Pantothenate Synthetase From M. Tuberculosis and Its Complexes with Substrates and A Reaction Intermediate Protein Sci. V. 12 1097 2003.
Page generated: Sat Oct 5 11:48:42 2024
ISSN: ISSN 0961-8368 PubMed: 12717031 DOI: 10.1110/PS.0241803 |
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