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Atomistry » Chlorine » PDB 3vfc-3vm5 » 3vm0 » |
Chlorine in PDB 3vm0: Assimilatory Nitrite Reductase (NII3) - N226K Mutant - NO2 Complex From Tobacco LeafEnzymatic activity of Assimilatory Nitrite Reductase (NII3) - N226K Mutant - NO2 Complex From Tobacco Leaf
All present enzymatic activity of Assimilatory Nitrite Reductase (NII3) - N226K Mutant - NO2 Complex From Tobacco Leaf:
1.7.7.1; Protein crystallography data
The structure of Assimilatory Nitrite Reductase (NII3) - N226K Mutant - NO2 Complex From Tobacco Leaf, PDB code: 3vm0
was solved by
S.Nakano,
M.Takahashi,
A.Sakamoto,
H.Morikawa,
K.Katayanagi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3vm0:
The structure of Assimilatory Nitrite Reductase (NII3) - N226K Mutant - NO2 Complex From Tobacco Leaf also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Assimilatory Nitrite Reductase (NII3) - N226K Mutant - NO2 Complex From Tobacco Leaf
(pdb code 3vm0). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Assimilatory Nitrite Reductase (NII3) - N226K Mutant - NO2 Complex From Tobacco Leaf, PDB code: 3vm0: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 3vm0Go back to![]() ![]()
Chlorine binding site 1 out
of 2 in the Assimilatory Nitrite Reductase (NII3) - N226K Mutant - NO2 Complex From Tobacco Leaf
![]() Mono view ![]() Stereo pair view
Chlorine binding site 2 out of 2 in 3vm0Go back to![]() ![]()
Chlorine binding site 2 out
of 2 in the Assimilatory Nitrite Reductase (NII3) - N226K Mutant - NO2 Complex From Tobacco Leaf
![]() Mono view ![]() Stereo pair view
Reference:
S.Nakano,
M.Takahashi,
A.Sakamoto,
H.Morikawa,
K.Katayanagi.
X-Ray Crystal Structure of A Mutant Assimilatory Nitrite Reductase That Shows Sulfite Reductase-Like Activity Chem.Biodivers. V. 9 1989 2012.
Page generated: Sun Jul 21 07:04:20 2024
ISSN: ISSN 1612-1872 PubMed: 22976986 DOI: 10.1002/CBDV.201100442 |
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