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Magnesium in PDB 2wc5: Structure of Bmori GOBP2 (General Odorant Binding Protein 2)

Protein crystallography data

The structure of Structure of Bmori GOBP2 (General Odorant Binding Protein 2), PDB code: 2wc5 was solved by G.Robertson, J.-J.Zhou, X.He, J.A.Pickett, L.M.Field, N.H.Keep, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.60 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 33.160, 33.160, 189.672, 90.00, 90.00, 120.00
R / Rfree (%) 16.8 / 23.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Bmori GOBP2 (General Odorant Binding Protein 2) (pdb code 2wc5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of Bmori GOBP2 (General Odorant Binding Protein 2), PDB code: 2wc5:

Magnesium binding site 1 out of 1 in 2wc5

Go back to Magnesium Binding Sites List in 2wc5
Magnesium binding site 1 out of 1 in the Structure of Bmori GOBP2 (General Odorant Binding Protein 2)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Bmori GOBP2 (General Odorant Binding Protein 2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1142

b:19.6
occ:1.00
O A:HOH2064 2.0 16.1 1.0
O A:HOH2065 2.0 24.4 1.0
O A:HOH2099 2.1 31.9 1.0
O A:HOH2101 2.2 15.1 1.0
O A:HOH2102 2.2 12.9 1.0
OD1 A:ASP65 3.2 18.9 0.5
OD1 A:ASP107 3.9 17.7 1.0
O A:HOH2066 4.1 10.7 1.0
OD2 A:ASP107 4.3 17.0 1.0
CG A:ASP65 4.4 12.9 0.5
CG A:ASP107 4.5 14.3 1.0
O A:ASP65 4.6 9.9 1.0
NH1 A:ARG67 4.6 10.7 1.0
O A:HOH2063 4.7 29.2 1.0
O A:THR105 4.7 20.6 1.0
OD1 A:ASP65 5.0 14.1 0.5

Reference:

J.-J.Zhou, G.Robertson, X.He, S.Dufour, A.M.Hooper, J.A.Pickett, N.H.Keep, L.M.Field. Characterisation of Bombyx Mori Odorant-Binding Proteins Reveals That A General Odorant-Binding Protein Discriminates Between Sex Pheromone Components. J.Mol.Biol. V. 389 529 2009.
ISSN: ISSN 0022-2836
PubMed: 19371749
DOI: 10.1016/J.JMB.2009.04.015
Page generated: Wed Aug 14 06:02:27 2024

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