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Yttrium in PDB 3bof: Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ and Homocysteine

Enzymatic 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:

Resolution Low / High (Å) 46.68 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.067, 86.308, 125.879, 90.00, 100.03, 90.00
R / Rfree (%) 19.5 / 22.2

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:

Potassium (K) 2 atoms
Zinc (Zn) 2 atoms

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 3bof

Go 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

A full contact list of Yttrium with other atoms in the Y binding site number 1 of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ and Homocysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Y705

b:41.0
occ:1.00
OE2 A:GLU421 2.5 34.6 1.0
O A:HOH908 2.5 32.6 1.0
OE1 A:GLU421 2.6 35.3 1.0
O A:HOH997 2.9 42.6 1.0
CD A:GLU421 2.9 34.6 1.0
CG A:GLU421 4.3 31.0 1.0
NE2 A:HIS464 4.7 32.2 1.0

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.
ISSN: ISSN 0027-8424
PubMed: 18296644
DOI: 10.1073/PNAS.0709960105
Page generated: Wed Dec 16 02:40:53 2020

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