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Atomistry » Magnesium » PDB 3f2t-3fcv » 3fbw » |
Magnesium in PDB 3fbw: Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Dhaa Mutant C176YEnzymatic activity of Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Dhaa Mutant C176Y
All present enzymatic activity of Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Dhaa Mutant C176Y:
3.8.1.5; Protein crystallography data
The structure of Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Dhaa Mutant C176Y, PDB code: 3fbw
was solved by
J.Dohnalek,
A.Stsiapanava,
J.A.Gavira,
I.Kuta Smatanova,
M.Kuty,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3fbw:
The structure of Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Dhaa Mutant C176Y also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Dhaa Mutant C176Y
(pdb code 3fbw). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Dhaa Mutant C176Y, PDB code: 3fbw: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 3fbwGo back to Magnesium Binding Sites List in 3fbw
Magnesium binding site 1 out
of 2 in the Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Dhaa Mutant C176Y
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 3fbwGo back to Magnesium Binding Sites List in 3fbw
Magnesium binding site 2 out
of 2 in the Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Dhaa Mutant C176Y
Mono view Stereo pair view
Reference:
A.Stsiapanava,
J.Dohnalek,
J.A.Gavira,
M.Kuty,
T.Koudelakova,
J.Damborsky,
I.Kuta Smatanova.
Atomic Resolution Studies of Haloalkane Dehalogenases DHAA04, DHAA14 and DHAA15 with Engineered Access Tunnels. Acta Crystallogr.,Sect.D V. 66 962 2010.
Page generated: Wed Aug 14 13:40:14 2024
ISSN: ISSN 0907-4449 PubMed: 20823547 DOI: 10.1107/S0907444910027101 |
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