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Sodium in PDB 5mig: The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 16-Th Structure of the Series with Total Exposition Time 453 Min. the Crystal Was Quick Refreezing Before This Data Collection.
Enzymatic activity of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 16-Th Structure of the Series with Total Exposition Time 453 Min. the Crystal Was Quick Refreezing Before This Data Collection.
All present enzymatic activity of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 16-Th Structure of the Series with Total Exposition Time 453 Min. the Crystal Was Quick Refreezing Before This Data Collection.:
1.10.3.2;
1.10.3.2;
Protein crystallography data
The structure of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 16-Th Structure of the Series with Total Exposition Time 453 Min. the Crystal Was Quick Refreezing Before This Data Collection., PDB code: 5mig
was solved by
K.M.Polyakov,
S.Gavryushov,
T.V.Fedorova,
O.A.Glazunova,
A.N.Popov,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 67.50 / 1.35 |
| Space group | P 21 21 21 |
| Cell size a, b, c (Å), α, β, γ (°) | 56.268, 84.415, 112.384, 90.00, 90.00, 90.00 |
| R / Rfree (%) | 14.1 / 16.2 |
Other elements in 5mig:
The structure of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 16-Th Structure of the Series with Total Exposition Time 453 Min. the Crystal Was Quick Refreezing Before This Data Collection. also contains other interesting chemical elements:
| Copper | (Cu) | 4 atoms |
Sodium Binding Sites:
The binding sites of Sodium atom in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 16-Th Structure of the Series with Total Exposition Time 453 Min. the Crystal Was Quick Refreezing Before This Data Collection.
(pdb code 5mig). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 16-Th Structure of the Series with Total Exposition Time 453 Min. the Crystal Was Quick Refreezing Before This Data Collection., PDB code: 5mig:
In total only one binding site of Sodium was determined in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 16-Th Structure of the Series with Total Exposition Time 453 Min. the Crystal Was Quick Refreezing Before This Data Collection., PDB code: 5mig:
Sodium binding site 1 out of 1 in 5mig
Go back to
Sodium Binding Sites List in 5mig
Sodium binding site 1 out
of 1 in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 16-Th Structure of the Series with Total Exposition Time 453 Min. the Crystal Was Quick Refreezing Before This Data Collection.
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Sodium with other atoms in the Na binding
site number 1 of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 16-Th Structure of the Series with Total Exposition Time 453 Min. the Crystal Was Quick Refreezing Before This Data Collection. within 5.0Å range:
|
Reference:
K.M.Polyakov,
S.Gavryushov,
S.Ivanova,
T.V.Fedorova,
O.A.Glazunova,
A.N.Popov,
O.V.Koroleva.
Structural Study of the X-Ray-Induced Enzymatic Reduction of Molecular Oxygen to Water By Steccherinum Murashkinskyi Laccase: Insights Into the Reaction Mechanism. Acta Crystallogr D Struct V. 73 388 2017BIOL.
ISSN: ISSN 2059-7983
PubMed: 28471364
DOI: 10.1107/S2059798317003667
Page generated: Mon Oct 7 22:41:09 2024
ISSN: ISSN 2059-7983
PubMed: 28471364
DOI: 10.1107/S2059798317003667
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