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Atomistry » Magnesium » PDB 1gq9-1h7q » 1gs6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1gq9-1h7q » 1gs6 » |
Magnesium in PDB 1gs6: Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite ReductaseEnzymatic activity of Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase
All present enzymatic activity of Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase:
1.7.2.1; 1.7.99.3; Protein crystallography data
The structure of Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase, PDB code: 1gs6
was solved by
M.J.Ellis,
M.Prudencio,
F.E.Dodd,
R.W.Strange,
G.Sawers,
R.R.Eady,
S.S.Hasnain,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1gs6:
The structure of Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase
(pdb code 1gs6). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase, PDB code: 1gs6: Magnesium binding site 1 out of 1 in 1gs6Go back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Crystal Structure of M144A Mutant of Alcaligenes Xylosoxidans Nitrite Reductase
![]() Mono view ![]() Stereo pair view
Reference:
M.J.Ellis,
M.Prudencio,
F.E.Dodd,
R.W.Strange,
G.Sawers,
R.R.Eady,
S.S.Hasnain.
Biochemical and Crystallographic Studies of the MET144ALA, ASP92ASN and HIS254PHE Mutants of the Nitrite Reductase From Alcaligenes Xylosoxidans Provide Insight Into the Enzyme Mechanism. J.Mol.Biol. V. 316 51 2002.
Page generated: Tue Aug 13 03:50:43 2024
ISSN: ISSN 0022-2836 PubMed: 11829502 DOI: 10.1006/JMBI.2001.5304 |
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