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

Enzymatic activity of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+

All present enzymatic activity of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+:
2.1.1.13;

Protein crystallography data

The structure of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+, PDB code: 3bol 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) 47.62 / 1.85
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.626, 85.841, 125.587, 90.00, 100.67, 90.00
R / Rfree (%) 19.3 / 22.8

Other elements in 3bol:

The structure of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ also contains other interesting chemical elements:

Potassium (K) 2 atoms
Zinc (Zn) 3 atoms

Yttrium Binding Sites:

The binding sites of Yttrium atom in the Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ (pdb code 3bol). 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+, PDB code: 3bol:

Yttrium binding site 1 out of 1 in 3bol

Go back to Yttrium Binding Sites List in 3bol
Yttrium binding site 1 out of 1 in the Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+


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+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Y705

b:34.7
occ:1.00
OD1 A:ASP253 2.2 19.6 1.0
O A:HOH804 3.1 37.8 1.0
CG A:ASP253 3.2 25.6 1.0
OD2 A:ASP253 3.4 30.0 1.0
ND1 A:HIS252 4.0 36.6 1.0
O A:HOH746 4.3 25.0 1.0
CB A:ASP253 4.5 23.0 1.0
CE1 A:HIS252 4.6 37.8 1.0
CA A:ASP253 4.8 22.6 1.0
N A:ASP253 4.9 23.1 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 02:40:54 2020

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