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Magnesium in PDB 2yje: Oligomeric Assembly of Actin Bound to Mrtf-A

Protein crystallography data

The structure of Oligomeric Assembly of Actin Bound to Mrtf-A, PDB code: 2yje was solved by S.Mouilleron, C.A.Langer, S.Guettler, N.Q.Mcdonald, R.Treisman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.88 / 3.10
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 90.935, 90.935, 321.613, 90.00, 90.00, 90.00
R / Rfree (%) 23.5 / 28

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Oligomeric Assembly of Actin Bound to Mrtf-A (pdb code 2yje). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Oligomeric Assembly of Actin Bound to Mrtf-A, PDB code: 2yje:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 2yje

Go back to Magnesium Binding Sites List in 2yje
Magnesium binding site 1 out of 3 in the Oligomeric Assembly of Actin Bound to Mrtf-A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Oligomeric Assembly of Actin Bound to Mrtf-A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg378

b:51.4
occ:1.00
O1B A:ATP377 2.3 70.6 1.0
O1G A:ATP377 2.9 70.4 1.0
OE1 A:GLN137 3.2 61.2 1.0
O3G A:ATP377 3.6 71.8 1.0
PB A:ATP377 3.7 69.5 1.0
PG A:ATP377 3.7 70.4 1.0
CD A:GLN137 3.8 59.4 1.0
OD1 A:ASP11 4.0 51.7 1.0
OD2 A:ASP11 4.1 57.8 1.0
O3B A:ATP377 4.2 68.9 1.0
OD2 A:ASP154 4.2 62.7 1.0
NE2 A:GLN137 4.3 59.0 1.0
O2B A:ATP377 4.4 70.2 1.0
O2A A:ATP377 4.4 71.0 1.0
CG A:ASP11 4.5 54.7 1.0
CA A:GLY13 4.7 38.3 1.0
O3A A:ATP377 4.8 69.9 1.0
CG A:GLN137 4.8 57.7 1.0
NZ A:LYS18 4.8 55.8 1.0
OD1 A:ASP154 4.9 67.3 1.0
CG A:ASP154 5.0 63.7 1.0
CB A:GLN137 5.0 57.5 1.0

Magnesium binding site 2 out of 3 in 2yje

Go back to Magnesium Binding Sites List in 2yje
Magnesium binding site 2 out of 3 in the Oligomeric Assembly of Actin Bound to Mrtf-A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Oligomeric Assembly of Actin Bound to Mrtf-A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg378

b:64.1
occ:1.00
O1B B:ATP377 2.3 83.1 1.0
O1G B:ATP377 2.7 82.8 1.0
PB B:ATP377 3.4 82.0 1.0
OE1 B:GLN137 3.5 0.8 1.0
PG B:ATP377 3.6 82.9 1.0
O3A B:ATP377 3.6 82.4 1.0
O3G B:ATP377 3.8 84.2 1.0
O3B B:ATP377 4.0 81.4 1.0
OD2 B:ASP154 4.1 0.0 1.0
CD B:GLN137 4.2 0.4 1.0
OD2 B:ASP11 4.3 90.1 1.0
OD1 B:ASP11 4.4 93.8 1.0
O2A B:ATP377 4.5 83.5 1.0
OD1 B:ASP154 4.6 0.3 1.0
NE2 B:GLN137 4.7 0.5 1.0
O2B B:ATP377 4.7 82.6 1.0
PA B:ATP377 4.8 83.0 1.0
CG B:ASP154 4.8 0.9 1.0
CG B:ASP11 4.8 91.3 1.0
NZ B:LYS18 4.8 85.1 1.0
CA B:GLY13 4.9 79.2 1.0
O2G B:ATP377 4.9 83.0 1.0
CA B:GLY156 5.0 74.5 1.0

Magnesium binding site 3 out of 3 in 2yje

Go back to Magnesium Binding Sites List in 2yje
Magnesium binding site 3 out of 3 in the Oligomeric Assembly of Actin Bound to Mrtf-A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Oligomeric Assembly of Actin Bound to Mrtf-A within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg378

b:45.7
occ:1.00
O1B C:ATP377 2.4 48.7 1.0
O1G C:ATP377 2.5 48.5 1.0
OE1 C:GLN137 3.4 68.1 1.0
PG C:ATP377 3.5 48.5 1.0
O3G C:ATP377 3.6 49.8 1.0
PB C:ATP377 3.7 47.6 1.0
CD C:GLN137 4.0 69.2 1.0
O3B C:ATP377 4.1 47.0 1.0
OD2 C:ASP11 4.1 50.5 1.0
OD1 C:ASP11 4.2 50.8 1.0
OD2 C:ASP154 4.3 67.7 1.0
O2B C:ATP377 4.3 48.2 1.0
NE2 C:GLN137 4.4 70.4 1.0
CG C:ASP11 4.6 50.7 1.0
O2A C:ATP377 4.6 49.1 1.0
CA C:GLY13 4.6 70.9 1.0
NZ C:LYS18 4.7 50.4 1.0
O2G C:ATP377 4.9 48.6 1.0
OD1 C:ASP154 4.9 65.5 1.0
O3A C:ATP377 4.9 48.0 1.0
CG C:GLN137 4.9 69.5 1.0

Reference:

S.Mouilleron, C.A.Langer, S.Guettler, N.Q.Mcdonald, R.Treisman. Structure of A Pentavalent G-Actin*Mrtf-A Complex Reveals How G-Actin Controls Nucleocytoplasmic Shuttling of A Transcriptional Coactivator. Sci Signal V. 4 RA40 2011.
ISSN: ESSN 1937-9145
PubMed: 21673315
DOI: 10.1126/SCISIGNAL.2001750
Page generated: Mon Dec 14 07:49:04 2020

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