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Atomistry » Chlorine » PDB 1o54-1ome » 1oah | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 1o54-1ome » 1oah » |
Chlorine in PDB 1oah: Cytochrome C Nitrite Reductase From Desulfovibrio Desulfuricans Atcc 27774: the Relevance of the Two Calcium Sites in the Structure of the Catalytic Subunit (Nrfa).Enzymatic activity of Cytochrome C Nitrite Reductase From Desulfovibrio Desulfuricans Atcc 27774: the Relevance of the Two Calcium Sites in the Structure of the Catalytic Subunit (Nrfa).
All present enzymatic activity of Cytochrome C Nitrite Reductase From Desulfovibrio Desulfuricans Atcc 27774: the Relevance of the Two Calcium Sites in the Structure of the Catalytic Subunit (Nrfa).:
1.7.2.2; Protein crystallography data
The structure of Cytochrome C Nitrite Reductase From Desulfovibrio Desulfuricans Atcc 27774: the Relevance of the Two Calcium Sites in the Structure of the Catalytic Subunit (Nrfa)., PDB code: 1oah
was solved by
C.A.Cunha,
S.Macieira,
J.M.Dias,
G.Almeida,
L.L.Goncalves,
C.Costa,
J.Lampreia,
R.Huber,
J.J.G.Moura,
I.Moura,
M.J.Romao,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1oah:
The structure of Cytochrome C Nitrite Reductase From Desulfovibrio Desulfuricans Atcc 27774: the Relevance of the Two Calcium Sites in the Structure of the Catalytic Subunit (Nrfa). also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Cytochrome C Nitrite Reductase From Desulfovibrio Desulfuricans Atcc 27774: the Relevance of the Two Calcium Sites in the Structure of the Catalytic Subunit (Nrfa).
(pdb code 1oah). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Cytochrome C Nitrite Reductase From Desulfovibrio Desulfuricans Atcc 27774: the Relevance of the Two Calcium Sites in the Structure of the Catalytic Subunit (Nrfa)., PDB code: 1oah: Jump to Chlorine binding site number: 1; 2; 3; 4; Chlorine binding site 1 out of 4 in 1oahGo back to Chlorine Binding Sites List in 1oah
Chlorine binding site 1 out
of 4 in the Cytochrome C Nitrite Reductase From Desulfovibrio Desulfuricans Atcc 27774: the Relevance of the Two Calcium Sites in the Structure of the Catalytic Subunit (Nrfa).
Mono view Stereo pair view
Chlorine binding site 2 out of 4 in 1oahGo back to Chlorine Binding Sites List in 1oah
Chlorine binding site 2 out
of 4 in the Cytochrome C Nitrite Reductase From Desulfovibrio Desulfuricans Atcc 27774: the Relevance of the Two Calcium Sites in the Structure of the Catalytic Subunit (Nrfa).
Mono view Stereo pair view
Chlorine binding site 3 out of 4 in 1oahGo back to Chlorine Binding Sites List in 1oah
Chlorine binding site 3 out
of 4 in the Cytochrome C Nitrite Reductase From Desulfovibrio Desulfuricans Atcc 27774: the Relevance of the Two Calcium Sites in the Structure of the Catalytic Subunit (Nrfa).
Mono view Stereo pair view
Chlorine binding site 4 out of 4 in 1oahGo back to Chlorine Binding Sites List in 1oah
Chlorine binding site 4 out
of 4 in the Cytochrome C Nitrite Reductase From Desulfovibrio Desulfuricans Atcc 27774: the Relevance of the Two Calcium Sites in the Structure of the Catalytic Subunit (Nrfa).
Mono view Stereo pair view
Reference:
C.A.Cunha,
S.Macieira,
J.M.Dias,
G.Almeida,
L.L.Goncalves,
C.Costa,
J.Lampreia,
R.Huber,
J.J.G.Moura,
I.Moura,
M.J.Romao.
Cytochrome C Nitrite Reductase From Desulfovibrio Desulfuricans Atcc 27774. the Relevance of the Two Calcium Sites in the Structure of the Catalytic Subunit (Nrfa) J.Biol.Chem. V. 278 17455 2003.
Page generated: Sat Jul 20 00:51:53 2024
ISSN: ISSN 0021-9258 PubMed: 12618432 DOI: 10.1074/JBC.M211777200 |
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