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Magnesium in PDB 2wmo: Structure of the Complex Between DOCK9 and CDC42.

Protein crystallography data

The structure of Structure of the Complex Between DOCK9 and CDC42., PDB code: 2wmo was solved by J.Yang, S.M.Roe, D.Barford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.990 / 2.20
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 93.060, 88.590, 89.980, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 27.18

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Complex Between DOCK9 and CDC42. (pdb code 2wmo). 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 the Complex Between DOCK9 and CDC42., PDB code: 2wmo:

Magnesium binding site 1 out of 1 in 2wmo

Go back to Magnesium Binding Sites List in 2wmo
Magnesium binding site 1 out of 1 in the Structure of the Complex Between DOCK9 and CDC42.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Complex Between DOCK9 and CDC42. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1179

b:46.4
occ:1.00
O3G B:GTP1178 2.6 47.4 1.0
O1B B:GTP1178 2.8 39.6 1.0
O1A B:GTP1178 2.8 41.3 1.0
O B:HOH2070 2.8 44.4 1.0
OG1 B:THR17 2.8 42.1 1.0
CB B:THR17 3.3 36.4 1.0
O3B B:GTP1178 3.4 40.9 1.0
PG B:GTP1178 3.5 48.0 1.0
PB B:GTP1178 3.6 41.8 1.0
PA B:GTP1178 3.8 41.9 1.0
O B:HOH2072 3.8 49.2 1.0
O B:HOH2069 3.8 43.1 1.0
O3A B:GTP1178 4.1 45.8 1.0
CG2 B:THR17 4.1 35.8 1.0
O2A B:GTP1178 4.1 38.9 1.0
O2G B:GTP1178 4.2 49.3 1.0
O B:HOH2073 4.3 45.4 1.0
CA B:THR17 4.6 37.1 1.0
N B:THR17 4.6 38.0 1.0
O B:HOH2008 4.8 64.4 1.0
O1G B:GTP1178 4.8 43.2 1.0
O2B B:GTP1178 5.0 42.4 1.0

Reference:

J.Yang, Z.Zhang, S.M.Roe, C.J.Marshall, D.Barford. Activation of Rho Gtpases By Dock Exchange Factors Is Mediated By A Nucleotide Sensor. Science V. 325 1398 2009.
ISSN: ISSN 0036-8075
PubMed: 19745154
DOI: 10.1126/SCIENCE.1174468
Page generated: Wed Aug 14 06:11:12 2024

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