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Magnesium in PDB 3g5s: Crystal Structure of Thermus Thermophilus Trmfo in Complex with Glutathione

Enzymatic activity of Crystal Structure of Thermus Thermophilus Trmfo in Complex with Glutathione

All present enzymatic activity of Crystal Structure of Thermus Thermophilus Trmfo in Complex with Glutathione:
2.1.1.74;

Protein crystallography data

The structure of Crystal Structure of Thermus Thermophilus Trmfo in Complex with Glutathione, PDB code: 3g5s was solved by H.Nishimasu, R.Ishitani, H.Hori, O.Nureki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.81 / 1.05
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.257, 92.226, 104.501, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 17.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Thermus Thermophilus Trmfo in Complex with Glutathione (pdb code 3g5s). 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 Thermus Thermophilus Trmfo in Complex with Glutathione, PDB code: 3g5s:

Magnesium binding site 1 out of 1 in 3g5s

Go back to Magnesium Binding Sites List in 3g5s
Magnesium binding site 1 out of 1 in the Crystal Structure of Thermus Thermophilus Trmfo in Complex with Glutathione


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 Thermus Thermophilus Trmfo in Complex with Glutathione within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg446

b:16.1
occ:0.81
O32 A:GSH445 2.1 19.5 0.8
OE1 A:GLN391 2.2 9.5 0.4
O A:HOH636 2.3 29.1 1.0
O A:HOH634 2.3 29.0 1.0
O A:HOH635 2.3 29.1 1.0
O A:HOH637 2.4 29.1 1.0
C3 A:GSH445 3.1 18.6 0.8
CD A:GLN391 3.2 9.7 0.4
O31 A:GSH445 3.4 19.1 0.9
NE2 A:GLN391 3.5 9.9 0.4
CG A:GLN391 3.9 12.8 0.6
O A:GLY389 4.1 13.6 1.0
OE2 A:GLU265 4.1 18.2 1.0
O A:HOH481 4.2 34.3 1.0
OG A:SER161 4.2 11.9 0.7
O A:HOH791 4.2 21.5 1.0
OG A:SER273 4.2 13.6 1.0
NH2 A:ARG263 4.4 18.0 1.0
O A:HOH480 4.4 31.1 1.0
O A:HOH815 4.4 19.4 1.0
CA3 A:GSH445 4.5 18.1 0.9
CG A:GLN391 4.5 10.1 0.4
CB A:SER273 4.7 12.3 1.0
CZ A:ARG263 4.7 18.1 1.0
N A:SER161 4.8 11.9 1.0
NE A:ARG263 4.8 18.7 1.0
N3 A:GSH445 4.8 17.6 0.9
CD A:GLN391 4.9 13.6 0.6
CB A:GLN391 4.9 12.3 0.6
CB A:SER161 4.9 13.4 0.3
CD A:GLU265 4.9 15.2 1.0
OG A:SER161 4.9 14.2 0.3
CB A:GLN391 5.0 10.7 0.4

Reference:

H.Nishimasu, R.Ishitani, K.Yamashita, C.Iwashita, A.Hirata, H.Hori, O.Nureki. Atomic Structure of A Folate/Fad-Dependent Trna T54 Methyltransferase Proc.Natl.Acad.Sci.Usa V. 106 8180 2009.
ISSN: ISSN 0027-8424
PubMed: 19416846
DOI: 10.1073/PNAS.0901330106
Page generated: Wed Aug 14 14:05:54 2024

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