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Magnesium in PDB 3u9d: Crystal Structure of A Chimera Containing the N-Terminal Domain (Residues 8-24) of Drosophila Ciboulot and the C-Terminal Domain (Residues 13-44) of Bovine Thymosin-BETA4, Bound to G-Actin-Atp

Protein crystallography data

The structure of Crystal Structure of A Chimera Containing the N-Terminal Domain (Residues 8-24) of Drosophila Ciboulot and the C-Terminal Domain (Residues 13-44) of Bovine Thymosin-BETA4, Bound to G-Actin-Atp, PDB code: 3u9d was solved by L.Renault, C.Husson, M.F.Carlier, D.Didry, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.64 / 2.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 45.698, 75.738, 128.518, 90.00, 90.03, 90.00
R / Rfree (%) 20.4 / 24

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A Chimera Containing the N-Terminal Domain (Residues 8-24) of Drosophila Ciboulot and the C-Terminal Domain (Residues 13-44) of Bovine Thymosin-BETA4, Bound to G-Actin-Atp (pdb code 3u9d). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of A Chimera Containing the N-Terminal Domain (Residues 8-24) of Drosophila Ciboulot and the C-Terminal Domain (Residues 13-44) of Bovine Thymosin-BETA4, Bound to G-Actin-Atp, PDB code: 3u9d:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3u9d

Go back to Magnesium Binding Sites List in 3u9d
Magnesium binding site 1 out of 2 in the Crystal Structure of A Chimera Containing the N-Terminal Domain (Residues 8-24) of Drosophila Ciboulot and the C-Terminal Domain (Residues 13-44) of Bovine Thymosin-BETA4, Bound to G-Actin-Atp


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 A Chimera Containing the N-Terminal Domain (Residues 8-24) of Drosophila Ciboulot and the C-Terminal Domain (Residues 13-44) of Bovine Thymosin-BETA4, Bound to G-Actin-Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:28.8
occ:1.00
O1B A:ATP501 2.3 23.4 1.0
O3G A:ATP501 3.0 36.1 1.0
NE2 A:GLN137 3.5 17.8 1.0
PB A:ATP501 3.7 22.4 1.0
O3B A:ATP501 4.0 26.6 1.0
CD A:GLN137 4.0 16.5 1.0
PG A:ATP501 4.1 34.5 1.0
OE1 A:GLN137 4.2 17.1 1.0
OD2 A:ASP11 4.3 22.4 1.0
O1A A:ATP501 4.4 19.1 1.0
O1G A:ATP501 4.5 35.2 1.0
OD1 A:ASP11 4.5 27.0 1.0
O3A A:ATP501 4.5 22.1 1.0
OD1 A:ASP154 4.6 25.4 1.0
CG2 A:VAL339 4.6 12.1 1.0
OD2 A:ASP154 4.8 25.3 1.0
CG A:ASP11 4.8 25.8 1.0
O2B A:ATP501 4.8 24.8 1.0
PA A:ATP501 5.0 20.2 1.0

Magnesium binding site 2 out of 2 in 3u9d

Go back to Magnesium Binding Sites List in 3u9d
Magnesium binding site 2 out of 2 in the Crystal Structure of A Chimera Containing the N-Terminal Domain (Residues 8-24) of Drosophila Ciboulot and the C-Terminal Domain (Residues 13-44) of Bovine Thymosin-BETA4, Bound to G-Actin-Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of A Chimera Containing the N-Terminal Domain (Residues 8-24) of Drosophila Ciboulot and the C-Terminal Domain (Residues 13-44) of Bovine Thymosin-BETA4, Bound to G-Actin-Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg502

b:17.2
occ:1.00
O3G C:ATP501 2.2 32.0 1.0
O1B C:ATP501 2.5 27.7 1.0
O1G C:ATP501 2.5 35.0 1.0
PG C:ATP501 2.8 33.6 1.0
OD1 C:ASP11 3.0 25.0 1.0
CA C:GLY13 3.2 25.8 1.0
OE1 C:GLN137 3.5 10.8 1.0
PB C:ATP501 3.6 28.2 1.0
O3B C:ATP501 3.7 29.3 1.0
NE2 C:GLN137 3.7 7.6 1.0
CD C:GLN137 3.7 8.8 1.0
CG C:ASP11 3.7 24.4 1.0
OD2 C:ASP11 3.8 24.1 1.0
O C:ASN12 3.8 25.5 1.0
N C:GLY13 3.8 25.9 1.0
C C:ASN12 4.0 25.7 1.0
O2G C:ATP501 4.2 34.9 1.0
C C:GLY13 4.4 25.8 1.0
NZ C:LYS18 4.5 24.9 1.0
O2B C:ATP501 4.5 21.9 1.0
N C:SER14 4.5 26.2 1.0
O3A C:ATP501 4.7 29.0 1.0
CE C:LYS18 4.8 23.1 1.0
CG C:GLN137 4.8 11.4 1.0

Reference:

D.Didry, F.X.Cantrelle, C.Husson, P.Roblin, A.M.Moorthy, J.Perez, C.Le Clainche, M.Hertzog, E.Guittet, M.F.Carlier, C.Van Heijenoort, L.Renault. How A Single Residue in Individual Beta-Thymosin/WH2 Domains Controls Their Functions in Actin Assembly. Embo J. V. 31 1000 2012.
ISSN: ISSN 0261-4189
PubMed: 22193718
DOI: 10.1038/EMBOJ.2011.461
Page generated: Thu Aug 15 12:26:51 2024

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