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Magnesium in PDB 1o1t: Structure of Fpt Bound to the Cvim-Fpp Product

Protein crystallography data

The structure of Structure of Fpt Bound to the Cvim-Fpp Product, PDB code: 1o1t was solved by T.C.Turek-Etienne, C.L.Strickland, M.D.Distefano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.10
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 171.440, 171.440, 69.220, 90.00, 90.00, 120.00
R / Rfree (%) 19.8 / n/a

Other elements in 1o1t:

The structure of Structure of Fpt Bound to the Cvim-Fpp Product also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Fpt Bound to the Cvim-Fpp Product (pdb code 1o1t). 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 Fpt Bound to the Cvim-Fpp Product, PDB code: 1o1t:

Magnesium binding site 1 out of 1 in 1o1t

Go back to Magnesium Binding Sites List in 1o1t
Magnesium binding site 1 out of 1 in the Structure of Fpt Bound to the Cvim-Fpp Product


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Fpt Bound to the Cvim-Fpp Product within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1001

b:26.9
occ:1.00
O B:HOH3028 2.0 22.9 1.0
O B:HOH3011 2.3 19.4 1.0
NE2 B:HIS194 2.3 31.7 1.0
OE1 B:GLU198 2.7 54.9 1.0
CD2 B:HIS194 3.2 31.1 1.0
CE1 B:HIS194 3.2 34.9 1.0
CD B:GLU198 3.7 53.6 1.0
OE2 B:GLU198 4.0 52.2 1.0
CA B:GLY197 4.2 32.6 1.0
CB A:TYR131 4.2 21.6 1.0
O A:HOH380 4.4 21.5 1.0
ND1 B:HIS194 4.4 33.6 1.0
CD2 A:HIS170 4.4 25.0 1.0
CG B:HIS194 4.4 31.5 1.0
CG A:GLN167 4.4 19.2 1.0
NE2 A:GLN167 4.5 29.4 1.0
N B:GLU198 4.5 34.9 1.0
CG A:HIS170 4.7 26.2 1.0
NE2 B:HIS149 4.8 20.6 1.0
CB A:HIS170 4.9 21.2 1.0
C B:GLY197 4.9 34.8 1.0
CD A:GLN167 5.0 25.5 1.0

Reference:

T.C.Turek-Etienne, C.L.Strickland, M.D.Distefano. Biochemical and Structural Studies with Prenyl Diphosphate Analogues Provide Insights Into Isoprenoid Recognition By Protein Farnesyl Transferase Biochemistry V. 42 3716 2003.
ISSN: ISSN 0006-2960
PubMed: 12667062
DOI: 10.1021/BI0266838
Page generated: Tue Aug 13 10:31:55 2024

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