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Magnesium in PDB 3rrm: S. Cerevisiae DBP5 L327V Bound to NUP159, GLE1 H337R, IP6 and Adp

Enzymatic activity of S. Cerevisiae DBP5 L327V Bound to NUP159, GLE1 H337R, IP6 and Adp

All present enzymatic activity of S. Cerevisiae DBP5 L327V Bound to NUP159, GLE1 H337R, IP6 and Adp:
3.6.4.13;

Protein crystallography data

The structure of S. Cerevisiae DBP5 L327V Bound to NUP159, GLE1 H337R, IP6 and Adp, PDB code: 3rrm was solved by B.Montpetit, N.D.Thomsen, K.J.Helmke, M.A.Seeliger, J.M.Berger, K.Weis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.27 / 2.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 186.912, 67.982, 132.392, 90.00, 127.52, 90.00
R / Rfree (%) 22.9 / 26.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the S. Cerevisiae DBP5 L327V Bound to NUP159, GLE1 H337R, IP6 and Adp (pdb code 3rrm). 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 S. Cerevisiae DBP5 L327V Bound to NUP159, GLE1 H337R, IP6 and Adp, PDB code: 3rrm:

Magnesium binding site 1 out of 1 in 3rrm

Go back to Magnesium Binding Sites List in 3rrm
Magnesium binding site 1 out of 1 in the S. Cerevisiae DBP5 L327V Bound to NUP159, GLE1 H337R, IP6 and Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of S. Cerevisiae DBP5 L327V Bound to NUP159, GLE1 H337R, IP6 and Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg2

b:51.0
occ:1.00
O32 B:IHP1 2.0 0.9 1.0
O23 B:IHP1 2.2 57.8 1.0
P3 B:IHP1 3.5 59.5 1.0
P2 B:IHP1 3.5 56.8 1.0
O43 B:IHP1 3.7 62.6 1.0
O42 B:IHP1 4.0 57.7 1.0
NZ B:LYS401 4.1 64.6 1.0
O13 B:IHP1 4.2 58.0 1.0
O22 B:IHP1 4.2 1.0 1.0
CD B:ARG337 4.3 49.7 1.0
C2 B:IHP1 4.4 56.2 1.0
O41 B:IHP1 4.4 59.6 1.0
O12 B:IHP1 4.5 56.3 1.0
O33 B:IHP1 4.6 58.9 1.0
C3 B:IHP1 4.7 57.0 1.0

Reference:

B.Montpetit, N.D.Thomsen, K.J.Helmke, M.A.Seeliger, J.M.Berger, K.Weis. A Conserved Mechanism of Dead-Box Atpase Activation By Nucleoporins and INSP6 in Mrna Export. Nature V. 472 238 2011.
ISSN: ISSN 0028-0836
PubMed: 21441902
DOI: 10.1038/NATURE09862
Page generated: Thu Aug 15 10:36:50 2024

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