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Atomistry » Yttrium » PDB 1dde-3ph5 » 3bof | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Yttrium » PDB 1dde-3ph5 » 3bof » |
Yttrium in PDB 3bof: Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ and HomocysteineEnzymatic activity of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ and Homocysteine
All present enzymatic activity of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ and Homocysteine:
2.1.1.13; Protein crystallography data
The structure of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ and Homocysteine, PDB code: 3bof
was solved by
M.Koutmos,
J.L.Smith,
M.L.Ludwig,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3bof:
The structure of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ and Homocysteine also contains other interesting chemical elements:
Yttrium Binding Sites:
The binding sites of Yttrium atom in the Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ and Homocysteine
(pdb code 3bof). This binding sites where shown within
5.0 Angstroms radius around Yttrium atom.
In total only one binding site of Yttrium was determined in the Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ and Homocysteine, PDB code: 3bof: Yttrium binding site 1 out of 1 in 3bofGo back to Yttrium Binding Sites List in 3bof
Yttrium binding site 1 out
of 1 in the Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ and Homocysteine
Mono view Stereo pair view
Reference:
M.Koutmos,
R.Pejchal,
T.M.Bomer,
R.G.Matthews,
J.L.Smith,
M.L.Ludwig.
Metal Active Site Elasticity Linked to Activation of Homocysteine in Methionine Synthases. Proc.Natl.Acad.Sci.Usa V. 105 3286 2008.
Page generated: Sat Oct 12 20:31:41 2024
ISSN: ISSN 0027-8424 PubMed: 18296644 DOI: 10.1073/PNAS.0709960105 |
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