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Magnesium in PDB 5jxm: Crystal Structure of Prenyltransferase Prib Apo Form

Protein crystallography data

The structure of Crystal Structure of Prenyltransferase Prib Apo Form, PDB code: 5jxm was solved by H.Cao, S.Elshahawi, J.Benach, S.R.Wasserman, L.L.Morisco, J.W.Koss, J.S.Thorson, G.N.Phillips Jr., Enzyme Discovery For Natural Productbiosynthesis (Natpro), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.56 / 1.15
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 103.526, 83.723, 41.527, 90.00, 106.27, 90.00
R / Rfree (%) 17.9 / 21.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Prenyltransferase Prib Apo Form (pdb code 5jxm). 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 Crystal Structure of Prenyltransferase Prib Apo Form, PDB code: 5jxm:

Magnesium binding site 1 out of 1 in 5jxm

Go back to Magnesium Binding Sites List in 5jxm
Magnesium binding site 1 out of 1 in the Crystal Structure of Prenyltransferase Prib Apo Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Prenyltransferase Prib Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:37.3
occ:1.00
O A:HOH1127 2.1 41.5 1.0
O A:HOH672 2.2 47.4 1.0
O A:HOH1035 2.3 27.0 1.0
HB3 A:ASP210 3.3 26.0 1.0
O A:HOH1133 3.7 45.6 1.0
CB A:ASP210 4.1 21.7 1.0
HB2 A:ASP210 4.1 26.0 1.0
OD2 A:ASP210 4.4 25.4 1.0
O A:HOH695 4.4 23.3 1.0
O A:HOH666 4.5 34.2 1.0
CG A:ASP210 4.6 23.6 1.0
O A:HOH960 4.8 39.1 1.0

Reference:

S.I.Elshahawi, H.Cao, K.A.Shaaban, L.V.Ponomareva, T.Subramanian, M.L.Farman, H.P.Spielmann, G.N.Phillips, J.S.Thorson, S.Singh. Structure and Specificity of A Permissive Bacterial C-Prenyltransferase. Nat. Chem. Biol. V. 13 366 2017.
ISSN: ESSN 1552-4469
PubMed: 28166207
DOI: 10.1038/NCHEMBIO.2285
Page generated: Mon Dec 14 20:35:14 2020

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